SEARCH

Search Details

SUGASAWA Kaoru
Biosignal Research Center
Professor

Researcher basic information

■ Research news
  • 08 Dec. 2020, New findings shed light on the repair of UV-induced DNA damage　-The impact of the protein degradation system on DNA damage recognition and repair-
    Link to Kobe Univ. HP
  • 27 Apr. 2016, Mechanism revealed for repairing DNA damaged by UV radiation
    Link to Kobe Univ. HP
■ Research Keyword
  • cancer
  • xeroderma pigmentosum
  • DNA repair
■ Research Areas
  • Life sciences / Molecular biology
  • Life sciences / Genetics
  • Environmental science/Agricultural science / Environmental effects of chemicals
  • Environmental science/Agricultural science / Environmental effects of radiation

Research activity information

■ Paper
  • Masataka Akagawa, Kaoru Sugasawa, Kiyoe Ura, Akira Sassa
    The production of reactive oxygen species in response to RNA virus infection results in the oxidation of viral genomic RNA within infected cells. These oxidative RNA lesions undergo replication catalyzed by the viral replisome. G to U transversion mutations are frequently observed in the SARS-CoV-2 genome and may be linked to the replication process catalyzed by RNA-dependent RNA polymerase (RdRp) past the oxidative RNA lesion 7,8-dihydro-8-oxo-riboguanosine (8-oxo-rG). To better understand the mechanism of viral RNA mutagenesis, it is crucial to elucidate the role of RdRp in replicating across oxidative lesions. In this study, we investigated the RNA synthesis catalyzed by the reconstituted SARS-CoV-2 RdRp past a single 8-oxo-rG. The RdRp-mediated primer extension was significantly inhibited by 8-oxo-rG on the template RNA. A steady-state multiple-turnover reaction demonstrated that the turnover rate of RdRp was significantly slow when replication was blocked by 8-oxo-rG, reflecting low bypass efficiency even with prolonged reaction time. Once RdRp was able to bypass 8-oxo-rG, it preferentially incorporated rCMP, with a lesser amount of rAMP opposite 8-oxo-rG. In contrast, RdRp demonstrated greater activity in extending from the mutagenic rA:8-oxo-rG terminus compared to the lower efficiency of extension from the rC:8-oxo-rG pair. Based on steady-state kinetic analyses for the incorporation of rNMPs opposite 8-oxo-rG and chain extension from rC:8-oxo-rG or rA:8-oxo-rG, the relative bypass frequency for rA:8-oxo-rG was found to be seven-fold higher than that for rC:8-oxo-rG. Therefore, the properties of RdRp indicated in this study may contribute to the mechanism of mutagenesis of the SARS-CoV-2 genome.
    Apr. 2025, The Journal of biological chemistry, 108512 - 108512, English, International magazine
    Scientific journal

  • Tomoya Hotani, Motonari Goto, Yukie Otsuki, Shun Matsuda, Nobuhiro Wada, Masakazu Shinohara, Tomonari Matsuda, Masayuki Yokoi, Kaoru Sugasawa, Yuki Ohsaki, Wataru Sakai
    Summary Fanconi anemia (FA) is a rare genetic disease caused by the loss of function of one of the 22 associated genes and is characterized by bone marrow failure, cancer predisposition, and developmental defects. The proteins encoded by these genes (FA proteins) mainly function in DNA damage response and repair. Although FA deficiency has multiple effects on the regulation of lipid metabolism, the molecular function of FA proteins in the context of FA pathology remains unclear. In the present study, we demonstrated that FANCD2, a key component of FA proteins, interacts with lipid metabolism-related factors and that FANCD2 deficiency downregulates the cellular levels of fatty acids. Moreover, a portion of FANCD2 is localized to nuclear lipid droplets in response to oleic acid treatment. These subcellular dynamics are independent of FANCD2 monoubiquitination, which is essential for the DNA damage response. Collectively, these findings demonstrate that FANCD2 responds to not only DNA damage but also oleic acid exposure, providing insights into the pathogenesis of lipid dysregulation in FA.
    Cold Spring Harbor Laboratory, Feb. 2025

  • ヌクレオチド除去修復のDNA損傷認識を制御するクロマチンダイナミクス
    日下部 将, 菅澤 薫
    Feb. 2025, 生化学, 97(1) (1), 61 - 65, Japanese
    [Refereed]
    Scientific journal

  • Satoshi Ninagawa, Masaki Matsuo, Deng Ying, Shuichiro Oshita, Shinya Aso, Kazutoshi Matsushita, Mai Taniguchi, Akane Fueki, Moe Yamashiro, Kaoru Sugasawa, Shunsuke Saito, Koshi Imami, Yasuhiko Kizuka, Tetsushi Sakuma, Takashi Yamamoto, Hirokazu Yagi, Koichi Kato, Kazutoshi Mori
    How the fate (folding versus degradation) of glycoproteins is determined in the endoplasmic reticulum (ER) is an intriguing question. Monoglucosylated glycoproteins are recognized by lectin chaperones to facilitate their folding, whereas glycoproteins exposing well-trimmed mannoses are subjected to glycoprotein ER-associated degradation (gpERAD); we have elucidated how mannoses are sequentially trimmed by EDEM family members (George et al., 2020; 2021 eLife). Although reglucosylation by UGGT was previously reported to have no effect on substrate degradation, here we directly tested this notion using cells with genetically disrupted UGGT1/2. Strikingly, the results showed that UGGT1 delayed the degradation of misfolded substrates and unstable glycoproteins including ATF6α. An experiment with a point mutant of UGGT1 indicated that the glucosylation activity of UGGT1 was required for the inhibition of early glycoprotein degradation. These and overexpression-based competition experiments suggested that the fate of glycoproteins is determined by a tug-of-war between structure formation by UGGT1 and degradation by EDEMs. We further demonstrated the physiological importance of UGGT1, since ATF6α cannot function properly without UGGT1. Thus, our work strongly suggests that UGGT1 is a central factor in ER protein quality control via the regulation of both glycoprotein folding and degradation.
    Dec. 2024, eLife, 12, English, International magazine
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Takeshi Yasuda, Nakako Nakajima, Tomoo Ogi, Tomoko Yanaka, Izumi Tanaka, Takaya Gotoh, Wataru Kagawa, Kaoru Sugasawa, Katsushi Tajima
    Oct. 2024, PLOS ONE
    Scientific journal

  • Takeshi Yasuda, Nakako Nakajima, Tomoko Yanaka, Takaya Gotoh, Wataru Kagawa, Kaoru Sugasawa, Katsushi Tajima
    Jul. 2023

  • Masayuki Kusakabe, Kaoru Sugasawa
    It remains uncertain how global genome nucleotide excision repair (GG-NER) efficiently removes various helix distorting DNA lesions in the cell nucleus. Here, we present a protocol to assess the contribution of factors of interest to GG-NER using two types of fluorescence-microscopy-based techniques. First, we describe steps for analyzing the localization of the factors upon local ultraviolet (UV) irradiation. We then detail the second technique, which quantifies the removal of UV-induced photolesions combined with lesion-specific antibodies and program-based image analysis. For complete details on the use and execution of this protocol, please refer to Kusakabe et al.1.
    Jun. 2023, STAR protocols, 4(3) (3), 102378 - 102378, English, International magazine
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Jun-ichi Akagi, Masayuki Yokoi, Yumi Miyake, Tsuyoshi Shirai, Tomohiro Baba, Young-Man Cho, Fumio Hanaoka, Kaoru Sugasawa, Shigenori Iwai, Kumiko Ogawa
    Elsevier BV, Jun. 2023, Journal of Biological Chemistry, 105002 - 105002
    Scientific journal

  • Jinseok Kim, Chia-Lung Li, Xuemin Chen, Yanxiang Cui, Filip M. Golebiowski, Huaibin Wang, Fumio Hanaoka, Kaoru Sugasawa, Wei Yang
    Springer Science and Business Media LLC, Apr. 2023, Nature, 617(7959) (7959), 170 - 175
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Hirotaka Kobayashi, Franklin Mayca Pozo, Wataru Sakai, Kenji Sato, Kaoru Sugasawa
    Nov. 2022, The Journal of Dermatology, 50(3) (3), 407 - 408, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Masayuki Kusakabe, Erina Kakumu, Fumika Kurihara, Kazuki Tsuchida, Takumi Maeda, Haruto Tada, Kanako Kusao, Akari Kato, Takeshi Yasuda, Tomonari Matsuda, Mitsuyoshi Nakao, Masayuki Yokoi, Wataru Sakai, Kaoru Sugasawa
    The XPC protein complex plays a central role in DNA lesion recognition for global genome nucleotide excision repair (GG-NER). Lesion recognition can be accomplished in either a UV-DDB-dependent or -independent manner; however, it is unclear how these sub-pathways are regulated in chromatin. Here, we show that histone deacetylases 1 and 2 facilitate UV-DDB-independent recruitment of XPC to DNA damage by inducing histone deacetylation. XPC localizes to hypoacetylated chromatin domains in a DNA damage-independent manner, mediated by its structurally disordered middle (M) region. The M region interacts directly with the N-terminal tail of histone H3, an interaction compromised by H3 acetylation. Although the M region is dispensable for in vitro NER, it promotes DNA damage removal by GG-NER in vivo, particularly in the absence of UV-DDB. We propose that histone deacetylation around DNA damage facilitates the recruitment of XPC through the M region, contributing to efficient lesion recognition and initiation of GG-NER.
    Elsevier BV, Apr. 2022, iScience, 25(4) (4), 104040 - 104040, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Takeshi Yasuda, Kazuya Takizawa, Ayako Ui, Michio Hama, Wataru Kagawa, Kaoru Sugasawa, Katsushi Tajima
    SIRT2 and SIRT3 protein deacetylases maintain genome integrity and stability. However, their mechanisms for maintaining the genome remain unclear. To examine the roles of SIRT2 and SIRT3 in DSB repair, I-SceI-based GFP reporter assays for HR, single-strand annealing (SSA) and nonhomologous end joining (NHEJ) repair were performed under SIRT2- or SIRT3-depleted conditions. SIRT2 or SIRT3 depletion inhibited HR repair equally to RAD52 depletion, but did not affect SSA and NHEJ repairs. SIRT2 or SIRT3 depletion disturbed the recruitment of RAD51 to DSB sites, an essential step for RAD51-dependent HR repair, but not directly through RAD52 deacetylation. SIRT2 or SIRT3 depletion decreased the colocalization of γH2AX foci with RPA1, and thus, they might be involved in initiating DSB end resection for the recruitment of RAD51 to DSB sites at an early step in HR repair. These results show the novel underlying mechanism of the SIRT2 and SIRT3 functions in HR for genome stability.
    Feb. 2021, Genes to cells : devoted to molecular & cellular mechanisms, 26(5) (5), 328 - 335, English, International magazine
    Scientific journal

  • Ying Zhang, Imke K Mandemaker, Syota Matsumoto, Oded Foreman, Christopher P Holland, Whitney R Lloyd, Kaoru Sugasawa, Wim Vermeulen, Jurgen A Marteijn, Paul J Galardy
    Nucleotide excision repair (NER) is a pathway involved in the repair of a variety of potentially mutagenic lesions that distort the DNA double helix. The ubiquitin E3-ligase complex UV-DDB is required for the recognition and repair of UV-induced cyclobutane pyrimidine dimers (CPDs) lesions through NER. DDB2 directly binds CPDs and subsequently undergoes ubiquitination and proteasomal degradation. DDB2 must remain on damaged chromatin, however, for sufficient time to recruit and hand-off lesions to XPC, a factor essential in the assembly of downstream repair components. Here we show that the tumor suppressor USP44 directly deubiquitinates DDB2 to prevent its premature degradation and is selectively required for CPD repair. Cells lacking USP44 have impaired DDB2 accumulation on DNA lesions with subsequent defects in XPC retention. The physiological importance of this mechanism is evident in that mice lacking Usp44 are prone to tumors induced by NER lesions introduced by DMBA or UV light. These data reveal the requirement for highly regulated ubiquitin addition and removal in the recognition and repair of helix-distorting DNA damage and identify another mechanism by which USP44 protects genomic integrity and prevents tumors.
    2021, Frontiers in cell and developmental biology, 9, 663411 - 663411, English, International magazine
    Scientific journal

  • Lu Chen, Rebecca R Bellone, Yan Wang, Moriel Singer-Berk, Kaoru Sugasawa, James M Ford, Steven E Artandi
    Squamous cell carcinoma (SCC) occurs frequently in the human Xeroderma Pigmentosum (XP) syndrome and is characterized by deficient UV-damage repair. SCC is the most common equine ocular cancer and the only associated genetic risk factor is a UV-damage repair protein. Specifically, a missense mutation in horse DDB2 (T338M) was strongly associated with both limbal SCC and third eyelid SCC in three breeds of horses (Halflinger, Belgian, and Rocky Mountain Horses) and was hypothesized to impair binding to UV-damaged DNA. Here, we investigate DDB2-T338M mutant's capacity to recognize UV lesions in vitro and in vivo, together with human XP mutants DDB2-R273H and -K244E. We show that the recombinant DDB2-T338M assembles with DDB1, but fails to show any detectable binding to DNA substrates with or without UV lesions, due to a potential structural disruption of the rigid DNA recognition β-loop. Consistently, we demonstrate that the cellular DDB2-T338M is defective in its recruitment to focally radiated DNA damages, and in its access to chromatin. Thus, we provide direct functional evidence indicating the DDB2-T338M recapitulates molecular defects of human XP mutants, and is the causal loss-of-function allele that gives rise to equine ocular SCCs. Our findings shed new light on the mechanism of DNA recognition by UV-DDB and on the initiation of ocular malignancy.
    Jan. 2021, DNA repair, 97, 103022 - 103022, English, International magazine
    Scientific journal

  • Wataru Sakai, Mayumi Yuasa-Sunagawa, Masayuki Kusakabe, Aiko Kishimoto, Takeshi Matsui, Yuki Kaneko, Jun-Ichi Akagi, Nicolas Huyghe, Masae Ikura, Tsuyoshi Ikura, Fumio Hanaoka, Masayuki Yokoi, Kaoru Sugasawa
    The ubiquitin-proteasome system (UPS) plays crucial roles in regulation of various biological processes, including DNA repair. In mammalian global genome nucleotide excision repair (GG-NER), activation of the DDB2-associated ubiquitin ligase upon UV-induced DNA damage is necessary for efficient recognition of lesions. To date, however, the precise roles of UPS in GG-NER remain incompletely understood. Here, we show that the proteasome subunit PSMD14 and the UPS shuttle factor RAD23B can be recruited to sites with UV-induced photolesions even in the absence of XPC, suggesting that proteolysis occurs at DNA damage sites. Unexpectedly, sustained inhibition of proteasome activity results in aggregation of PSMD14 (presumably with other proteasome components) at the periphery of nucleoli, by which DDB2 is immobilized and sequestered from its lesion recognition functions. Although depletion of PSMD14 alleviates such DDB2 immobilization induced by proteasome inhibitors, recruitment of DDB2 to DNA damage sites is then severely compromised in the absence of PSMD14. Because all of these proteasome dysfunctions selectively impair removal of cyclobutane pyrimidine dimers, but not (6-4) photoproducts, our results indicate that the functional integrity of the proteasome is essential for the DDB2-mediated lesion recognition sub-pathway, but not for GG-NER initiated through direct lesion recognition by XPC.
    Nov. 2020, Scientific Reports, 10(1) (1), 19704 - 19704, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Ayuna Takeishi, Hiroyuki Kogashi, Mizuki Odagiri, Hiroyuki Sasanuma, Shunichi Takeda, Manabu Yasui, Masamitsu Honma, Tetsuya Suzuki, Hiroyuki Kamiya, Kaoru Sugasawa, Kiyoe Ura, Akira Sassa
    Ribonucleoside triphosphates are often incorporated into genomic DNA during DNA replication. The accumulation of unrepaired ribonucleotides is associated with genomic instability, which is mediated by DNA topoisomerase 1 (Top1) processing of embedded ribonucleotides. The cleavage initiated by Top1 at the site of a ribonucleotide leads to the formation of a Top1-DNA cleavage complex (Top1cc), occasionally resulting in a DNA double-strand break (DSB). In humans, tyrosyl-DNA phosphodiesterases (TDPs) are essential repair enzymes that resolve the trapped Top1cc followed by downstream repair factors. However, there is limited cellular evidence of the involvement of TDPs in the processing of incorporated ribonucleotides in mammals. We assessed the role of TDPs in mutagenesis induced by a single ribonucleotide embedded into DNA. A supF shuttle vector site-specifically containing a single riboguanosine (rG) was introduced into the human lymphoblastoid TK6 cell line and its TDP1-, TDP2-, and TDP1/TDP2-deficient derivatives. TDP1 and TDP2 insufficiency remarkably decreased the mutant frequency caused by an embedded rG. The ratio of large deletion mutations induced by rG was also substantially lower in TDP1/TDP2-deficient cells than wild-type cells. Furthermore, the disruption of TDPs reduced the length of rG-mediated large deletion mutations. The recovery ratio of the propagated plasmid was also increased in TDP1/TDP2-deficient cells after the transfection of the shuttle vector containing rG. The results suggest that TDPs-mediated ribonucleotide processing cascade leads to unfavorable consequences, whereas in the absence of these repair factors, a more error-free processing pathway might function to suppress the ribonucleotide-induced mutagenesis. Furthermore, base substitution mutations at sites outside the position of rG were detected in the supF gene via a TDPs-independent mechanism. Overall, we provide new insights into the mechanism of mutagenesis induced by an embedded ribonucleotide in mammalian cells, which may lead to the fatal phenotype in the ribonucleotide excision repair deficiency.
    2020, PloS one, 15(12) (12), e0244790, English, International magazine
    Scientific journal

  • Ebtissal M Khouj, Suzanna L Prosser, Haruto Tada, Weng Man Chong, Jung-Chi Liao, Kaoru Sugasawa, Ciaran G Morrison
    Centrin 2 is a small conserved calcium-binding protein that localizes to the centriolar distal lumen in human cells. It is required for efficient primary ciliogenesis and nucleotide excision repair (NER). Centrin 2 forms part of the xeroderma pigmentosum group C protein complex. To explore how centrin 2 contributes to these distinct processes, we mutated the four calcium-binding EF-hand domains of human centrin 2. Centrin 2 in which all four EF-hands had been mutated to ablate calcium binding (4DA mutant) was capable of supporting in vitro NER and was as effective as the wild-type protein in rescuing the UV sensitivity of centrin 2-null cells. However, we found that mutation of any of the EF-hand domains impaired primary ciliogenesis in human TERT-RPE1 cells to the same extent as deletion of centrin 2. Phenotypic analysis of the 4DA mutant revealed defects in centrosome localization, centriole satellite assembly, ciliary assembly and function and in interactions with POC5 and SFI1. These observations indicate that centrin 2 requires calcium-binding capacity for its primary ciliogenesis functions, but not for NER, and suggest that these functions require centrin 2 to be capable of forming complexes with partner proteins.This article has an associated First Person interview with the first author of the paper.
    Oct. 2019, Journal of cell science, 132(19) (19), English, International magazine
    [Refereed]

  • Akira Sassa, Haruto Tada, Ayuna Takeishi, Kaho Harada, Megumi Suzuki, Masataka Tsuda, Hiroyuki Sasanuma, Shunichi Takeda, Kaoru Sugasawa, Manabu Yasui, Masamitsu Honma, Kiyoe Ura
    DNA polymerases often incorporate non-canonical nucleotide, i.e., ribonucleoside triphosphates into the genomic DNA. Aberrant accumulation of ribonucleotides in the genome causes various cellular abnormalities. Here, we show the possible role of human nucleotide excision repair (NER) and DNA polymerase η (Pol η) in processing of a single ribonucleotide embedded into DNA. We found that the reconstituted NER system can excise the oxidized ribonucleotide on the plasmid DNA. Taken together with the evidence that Pol η accurately bypasses a ribonucleotide, i.e., riboguanosine (rG) or its oxidized derivative (8-oxo-rG) in vitro, we further assessed the mutagenic potential of the embedded ribonucleotide in human cells lacking NER or Pol η. A single rG on the supF reporter gene predominantly induced large deletion mutations. An embedded 8-oxo-rG caused base substitution mutations at the 3'-neighboring base rather than large deletions in wild-type cells. The disruption of XPA, an essential factor for NER, or Pol η leads to the increased mutant frequency of 8-oxo-rG. Furthermore, the frequency of 8-oxo-rG-mediated large deletions was increased by the loss of Pol η, but not XPA. Collectively, our results suggest that base oxidation of the embedded ribonucleotide enables processing of the ribonucleotide via alternative DNA repair and damage tolerance pathways.
    Sep. 2019, Scientific reports, 9(1) (1), 13910 - 13910, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Publisher Correction: DNA damage detection in nucleosomes involves DNA register shifting.
    Matsumoto S, Cavadini S, Bunker RD, Grand RS, Potenza A, Rabl J, Yamamoto J, Schenk AD, Schübeler D, Iwai S, Sugasawa K, Kurumizaka H, Thomä NH
    Jul. 2019, Nature, 571(7764) (7764), E6, English
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • DNA damage detection in nucleosomes involves DNA register shifting.
    Matsumoto S, Cavadini S, Bunker RD, Grand RS, Potenza A, Rabl J, Yamamoto J, Schenk AD, Schübeler D, Iwai S, Sugasawa K, Kurumizaka H, Thomä NH
    Jul. 2019, Nature, 571(7763) (7763), 79 - 84, English
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Kaoru Sugasawa
    Nucleotide excision repair (NER) is a versatile DNA repair pathway that eliminates various helix-distorting base lesions such as ultraviolet (UV)-induced photolesions. Several recessive human disorders, such as xeroderma pigmentosum (XP), are caused by hereditary defects in NER, implying that the pathway plays critical roles in suppressing diverse pathogenic processes, including carcinogenesis. In general, discrimination of lesion sites from intact DNA, which is present in vast excess, is a key determinant of the overall efficiency of DNA repair. In mammalian cells, global genomic NER lesion recognition is initiated by the XPC protein complex, which achieves broad DNA-binding specificity by sensing destabilized base pairs rather than lesions per se. To avert unnecessary incisions at lesion-free sites, and thereby ensure the fidelity of the repair system, transcription factor IIH and the XPA protein then verify the presence of relevant lesions at suspicious sites bound by XPC. In the case of UV-induced photolesions, a specialized lesion sensor called UV-damaged DNA-binding protein (UV-DDB) contributes to efficient lesion recognition and the recruitment of XPC to lesion sites. The ubiquitin-proteasome system plays a crucial role in the handoff of lesions from UV-DDB to XPC and the subsequent NER process. In addition, recognition of lesions targeted by global genomic NER is intricately regulated by higher-order chromatin structures, which play distinct roles depending on the type of lesion.
    2019, The Enzymes, 45, 99 - 138, English, International magazine
    [Refereed]

  • Masayuki Kusakabe, Yuki Onishi, Haruto Tada, Fumika Kurihara, Kanako Kusao, Mari Furukawa, Shigenori Iwai, Masayuki Yokoi, Wataru Sakai, Kaoru Sugasawa
    Nucleotide excision repair (NER) is a versatile DNA repair pathway, which can remove an extremely broad range of base lesions from the genome. In mammalian global genomic NER, the XPC protein complex initiates the repair reaction by recognizing sites of DNA damage, and this depends on detection of disrupted/destabilized base pairs within the DNA duplex. A model has been proposed that XPC first interacts with unpaired bases and then the XPD ATPase/helicase in concert with XPA verifies the presence of a relevant lesion by scanning a DNA strand in 5'-3' direction. Such multi-step strategy for damage recognition would contribute to achieve both versatility and accuracy of the NER system at substantially high levels. In addition, recognition of ultraviolet light (UV)-induced DNA photolesions is facilitated by the UV-damaged DNA-binding protein complex (UV-DDB), which not only promotes recruitment of XPC to the damage sites, but also may contribute to remodeling of chromatin structures such that the DNA lesions gain access to XPC and the following repair proteins. Even in the absence of UV-DDB, however, certain types of histone modifications and/or chromatin remodeling could occur, which eventually enable XPC to find sites with DNA lesions. Exploration of novel factors involved in regulation of the DNA damage recognition process is now ongoing.
    BMC, 2019, Genes and environment : the official journal of the Japanese Environmental Mutagen Society, 41, 2 - 2, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Wataru Sakai, Kaoru Sugasawa
    Fanconi anemia (FA) is a rare genetic disease characterized by the deficiency of the cellular response and repair pathway for DNA interstrand crosslink (ICL) damage. Although recent studies have revealed the detailed molecular functions of FA proteins encoded by 22 genes, the mechanism of occurrence of endogenous ICLs in the human body remains poorly understood. In this short review, we summarize the potential endogenous sources of ICLs counteracted by FA proteins, and provide perspectives on the unanswered questions regarding FA.
    2019, Genes and environment : the official journal of the Japanese Environmental Mutagen Society, 41, 6 - 6, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • T. Masaki, E. Nakano, K. Okamura, R. Ono, K. Sugasawa, M. H. Lee, T. Suzuki, C. Nishigori
    Blackwell Publishing Ltd, Jun. 2018, British Journal of Dermatology, 178(6) (6), 1451 - 1452, English
    Scientific journal

  • Takeshi Yasuda, Wataru Kagawa, Tomoo Ogi, Takamitsu A Kato, Takehiro Suzuki, Naoshi Dohmae, Kazuya Takizawa, Yuka Nakazawa, Matthew D Genet, Mika Saotome, Michio Hama, Teruaki Konishi, Nakako Izumi Nakajima, Masaharu Hazawa, Masanori Tomita, Manabu Koike, Katsuko Noshiro, Kenichi Tomiyama, Chizuka Obara, Takaya Gotoh, Ayako Ui, Akira Fujimori, Fumiaki Nakayama, Fumio Hanaoka, Kaoru Sugasawa, Ryuichi Okayasu, Penny A Jeggo, Katsushi Tajima
    The p300 and CBP histone acetyltransferases are recruited to DNA double-strand break (DSB) sites where they induce histone acetylation, thereby influencing the chromatin structure and DNA repair process. Whether p300/CBP at DSB sites also acetylate non-histone proteins, and how their acetylation affects DSB repair, remain unknown. Here we show that p300/CBP acetylate RAD52, a human homologous recombination (HR) DNA repair protein, at DSB sites. Using in vitro acetylated RAD52, we identified 13 potential acetylation sites in RAD52 by a mass spectrometry analysis. An immunofluorescence microscopy analysis revealed that RAD52 acetylation at DSBs sites is counteracted by SIRT2- and SIRT3-mediated deacetylation, and that non-acetylated RAD52 initially accumulates at DSB sites, but dissociates prematurely from them. In the absence of RAD52 acetylation, RAD51, which plays a central role in HR, also dissociates prematurely from DSB sites, and hence HR is impaired. Furthermore, inhibition of ataxia telangiectasia mutated (ATM) protein by siRNA or inhibitor treatment demonstrated that the acetylation of RAD52 at DSB sites is dependent on the ATM protein kinase activity, through the formation of RAD52, p300/CBP, SIRT2, and SIRT3 foci at DSB sites. Our findings clarify the importance of RAD52 acetylation in HR and its underlying mechanism.
    Mar. 2018, PLoS genetics, 14(3) (3), e1007277, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Mutations at multiple CDK phosphorylation consensus sites on Cdt2 increase the affinity of CRL4Cdt2 for PCNA and its ubiquitination activity in S phase.
    Nukina, K, Hayashi, A, Shiomi, Y, Sugasawa, K, Ohtsubo, M, Nishitani, H
    Feb. 2018, Genes Cells, 23(3) (3), 200 - 213, English
    [Refereed]
    Scientific journal

  • Tomohumi Nakamura, Kouichi Murakami, Haruto Tada, Yoshihiko Uehara, Jumpei Nogami, Kazumitsu Maehara, Yasuyuki Ohkawa, Hisato Saitoh, Hideo Nishitani, Tetsuya Ono, Ryotaro Nishi, Masayuki Yokoi, Wataru Sakai, Kaoru Sugasawa
    Apr. 2017, GENES TO CELLS, 22(4) (4), 392 - 405, English
    [Refereed]
    Scientific journal

  • Philamer C. Calses, Kiranjit K. Dhillon, Nyka Tucker, Yong Chi, Jen-wei Huang, Masaoki Kawasumi, Paul Nghiem, Yemin Wang, Bruce E. Clurman, Celine Jacquemont, Philip R. Gafken, Kaoru Sugasawa, Masafumi Saijo, Toshiyasu Taniguchi
    Apr. 2017, CELL REPORTS, 19(1) (1), 162 - 174, English
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Erina Kakumu, Seiya Nakanishi, Hiromi M. Shiratori, Akari Kato, Wataru Kobayashi, Shinichi Machida, Takeshi Yasuda, Naoko Adachi, Naoaki Saito, Tsuyoshi Ikura, Hitoshi Kurumizaka, Hiroshi Kimura, Masayuki Yokoi, Wataru Sakai, Kaoru Sugasawa
    Mar. 2017, GENES TO CELLS, 22(3) (3), 310 - 327, English
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Miyuki Tanaka, Michiyo Takahara, Kohei Nukina, Akiyo Hayashi, Wataru Sakai, Kaoru Sugasawa, Yasushi Shiomi, Hideo Nishitani
    2017, CELL CYCLE, 16(7) (7), 673 - 684, English
    [Refereed]
    Scientific journal

  • Akihisa Osakabe, Yasuhiro Arimura, Syota Matsumoto, Naoki Horikoshi, Kaoru Sugasawa, Hitoshi Kurumizaka
    Jan. 2017, SCIENTIFIC REPORTS, 7(7) (7), 41783, English
    [Refereed]
    Scientific journal

  • Ryusuke Ono, Taro Masaki, Franklin Mayca Pozo, Yuka Nakazawa, Sigrid M A Swagemakers, Eiji Nakano, Wataru Sakai, Seiji Takeuchi, Fumio Kanda, Tomoo Ogi, Peter J van der Spek, Kaoru Sugasawa, Chikako Nishigori
    BACKGROUND: Most patients with xeroderma pigmentosum complementation group D (XP-D) from Western countries suffer from neurological symptoms, whereas Japanese patients display only skin manifestations without neurological symptoms. We have previously suggested that these differences in clinical manifestations in XP-D patients are attributed partly to a predominant mutation in ERCC2, and the allele frequency of S541R is highest in Japan. METHODS: We diagnosed a child with mild case of XP-D by the evaluation of DNA repair activity and whole-genome sequencing, and followed her ten years. RESULTS: Skin cancer, mental retardation, and neurological symptoms were not observed. Her minimal erythema dose was 41 mJ/cm(2) , which was slightly lower than that of healthy Japanese volunteers. The patient's cells showed sixfold hypersensitivity to UV in comparison with normal cells. Post-UV unscheduled DNA synthesis was 20.4%, and post-UV recovery of RNA synthesis was 58% of non-irradiated samples, which was lower than that of normal fibroblasts. Genome sequence analysis indicated that the patient harbored a compound heterozygous mutation of c.1621A>C and c.591_594del, resulting in p.S541R and p.Y197* in ERCC2: then, patient was diagnosed with XP-D. Y197* has not been described before. CONCLUSION: Her mild skin manifestations might be attributed to the mutational site on her genome and daily strict sun protection. c.1621A>C might be a founder mutation of ERCC2 among Japanese XP-D patients, as it was identified most frequently in Japanese XP-D patients and it has not been found elsewhere outside Japan.
    Jul. 2016, Photodermatology, photoimmunology & photomedicine, 32(4) (4), 174 - 80, English, International magazine
    [Refereed][Invited]
    Scientific journal

  • Simone Cavadini, Eric S. Fischer, Richard D. Bunker, Alessandro Potenza, Gondichatnahalli M. Lingaraju, Kenneth N. Goldie, Weaam I. Mohamed, Mahamadou Faty, Georg Petzold, Rohan E. J. Beckwith, Ritesh B. Tichkule, Ulrich Hassiepen, Wassim Abdulrahman, Radosav S. Pantelic, Syota Matsumoto, Kaoru Sugasawa, Henning Stahlberg, Nicolas H. Thomae
    Mar. 2016, NATURE, 531(7596) (7596), 598 - +, English
    [Refereed]
    Scientific journal

  • Simone Cavadini, Eric S. Fischer, Richard D. Bunker, Alessandro Potenza, Gondichatnahalli M. Lingaraju, Kenneth N. Goldie, Weaam I. Mohamed, Mahamadou Faty, Georg Petzold, Rohan E. J. Beckwith, Ritesh B. Tichkule, Ulrich Hassiepen, Wassim Abdulrahman, Radosav S. Pantelic, Syota Matsumoto, Kaoru Sugasawa, Henning Stahlberg, Nicolas H. Thomae
    Mar. 2016, NATURE, 531(7596) (7596), 598 - +, English
    Scientific journal

  • Naoki Horikoshi, Hiroaki Tachiwana, Wataru Kagawa, Akihisa Osakabe, Syota Matsumoto, Shigenori Iwai, Kaoru Sugasawa, Hitoshi Kurumizaka
    Feb. 2016, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 471(1) (1), 117 - 122, English
    [Refereed]
    Scientific journal

  • 2,2,4-Triamino-5(2H)-oxazolone is a weak substrate for nucleotide excision repair
    KinoK, Sugasawa Kaoru, MiyazawaH, HanaokaF
    Feb. 2016, Journal of pharmaceutical negative results, 7, 42 - 45, English
    [Refereed]
    Scientific journal

  • Katsuhito Kino, Kaoru Sugasawa, Hiroshi Miyazawa, Fumio Hanaoka
    Medknow Publications, Jan. 2016, Journal of Pharmaceutical Negative Results, 7(1) (1), 42 - 45, English
    [Refereed]
    Scientific journal

  • Akihisa Osakabe, Hiroaki Tachiwana, Wataru Kagawa, Naoki Horikoshi, Syota Matsumoto, Mayu Hasegawa, Naoyuki Matsumoto, Tatsuya Toga, Junpei Yamamoto, Fumio Hanaoka, Nicolas H Thomä, Kaoru Sugasawa, Shigenori Iwai, Hitoshi Kurumizaka
    UV-DDB, an initiation factor for the nucleotide excision repair pathway, recognizes 6-4PP lesions through a base flipping mechanism. As genomic DNA is almost entirely accommodated within nucleosomes, the flipping of the 6-4PP bases is supposed to be extremely difficult if the lesion occurs in a nucleosome, especially on the strand directly contacting the histone surface. Here we report that UV-DDB binds efficiently to nucleosomal 6-4PPs that are rotationally positioned on the solvent accessible or occluded surface. We determined the crystal structures of nucleosomes containing 6-4PPs in these rotational positions, and found that the 6-4PP DNA regions were flexibly disordered, especially in the strand exposed to the solvent. This characteristic of 6-4PP may facilitate UV-DDB binding to the damaged nucleosome. We present the first atomic-resolution pictures of the detrimental DNA cross-links of neighboring pyrimidine bases within the nucleosome, and provide the mechanistic framework for lesion recognition by UV-DDB in chromatin.
    Nov. 2015, Scientific reports, 5, 16330 - 16330, English, International magazine
    [Refereed]
    Scientific journal

  • Masahiko Okuda, Minoru Kinoshita, Erina Kakumu, Kaoru Sugasawa, Yoshifumi Nishimura
    Oct. 2015, STRUCTURE, 23(10) (10), 1827 - 1837, English
    [Refereed]
    Scientific journal

  • Chia-Lung Li, Filip M. Golebiowski, Yuki Onishi, Nadine L. Samara, Kaoru Sugasawa, Wei Yang
    Sep. 2015, MOLECULAR CELL, 59(6) (6), 1025 - 1034, English
    [Refereed]
    Scientific journal

  • Masaki Akita, Yon-Soo Tak, Tsutomu Shimura, Syota Matsumoto, Yuki Okuda-Shimizu, Yuichiro Shimizu, Ryotaro Nishi, Hisato Saitoh, Shigenori Iwai, Toshio Mori, Tsuyoshi Ikura, Wataru Sakai, Fumio Hanaoka, Kaoru Sugasawa
    The xeroderma pigmentosum group C (XPC) protein complex is a key factor that detects DNA damage and initiates nucleotide excision repair (NER) in mammalian cells. Although biochemical and structural studies have elucidated the interaction of XPC with damaged DNA, the mechanism of its regulation in vivo remains to be understood in more details. Here, we show that the XPC protein undergoes modification by small ubiquitin-related modifier (SUMO) proteins and the lack of this modification compromises the repair of UV-induced DNA photolesions. In the absence of SUMOylation, XPC is normally recruited to the sites with photolesions, but then immobilized profoundly by the UV-damaged DNA-binding protein (UV-DDB) complex. Since the absence of UV-DDB alleviates the NER defect caused by impaired SUMOylation of XPC, we propose that this modification is critical for functional interactions of XPC with UV-DDB, which facilitate the efficient damage handover between the two damage recognition factors and subsequent initiation of NER.
    Jun. 2015, Scientific reports, 5(5) (5), 10984 - 10984, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Masaki Akita, Yon-Soo Tak, Tsutomu Shimura, Syota Matsumoto, Yuki Okuda-Shimizu, Yuichiro Shimizu, Ryotaro Nishi, Hisato Saitoh, Shigenori Iwai, Toshio Mori, Tsuyoshi Ikura, Wataru Sakai, Fumio Hanaoka, Kaoru Sugasawa
    The xeroderma pigmentosum group C (XPC) protein complex is a key factor that detects DNA damage and initiates nucleotide excision repair (NER) in mammalian cells. Although biochemical and structural studies have elucidated the interaction of XPC with damaged DNA, the mechanism of its regulation in vivo remains to be understood in more details. Here, we show that the XPC protein undergoes modification by small ubiquitin-related modifier (SUMO) proteins and the lack of this modification compromises the repair of UV-induced DNA photolesions. In the absence of SUMOylation, XPC is normally recruited to the sites with photolesions, but then immobilized profoundly by the UV-damaged DNA-binding protein (UV-DDB) complex. Since the absence of UV-DDB alleviates the NER defect caused by impaired SUMOylation of XPC, we propose that this modification is critical for functional interactions of XPC with UV-DDB, which facilitate the efficient damage handover between the two damage recognition factors and subsequent initiation of NER.
    Jun. 2015, Scientific reports, 5, 10984 - 10984, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Okuda M, Kinoshita M, Kakumu E, Sugasawa K, Nishimura Y
    Jun. 2015, Structure, 5, 10984, English
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Structures of the nucleosomes containing UV-damaged DNA bases and the damaged base recognition mechanism by DNA repair proteins
    Akihisa Osakabe, Hiroaki Tachiwana, Naoki Horikoshi, Wataru Kagawa, Junpei Yamamoto, Takeshi Yasuda, Fumio Hanaoka, Kaoru Sugasawa, Shigenori Iwai, Hitoshi Kurumizaka
    Apr. 2015, DNA REPAIR, 28, 139 - 140, English

  • Yuko Kikuchi, Hiroyasu Umemura, Saori Nishitani, Satoshi Iida, Rikiya Fukasawa, Hiroto Hayashi, Yutaka Hirose, Aki Tanaka, Kaoru Sugasawa, Yoshiaki Ohkuma
    Mar. 2015, GENES TO CELLS, 20(3) (3), 191 - 202, English
    [Refereed]
    Scientific journal

  • Syota Matsumoto, Eric S Fischer, Takeshi Yasuda, Naoshi Dohmae, Shigenori Iwai, Toshio Mori, Ryotaro Nishi, Ken-ichi Yoshino, Wataru Sakai, Fumio Hanaoka, Nicolas H Thomä, Kaoru Sugasawa
    In mammalian nucleotide excision repair, the DDB1-DDB2 complex recognizes UV-induced DNA photolesions and facilitates recruitment of the XPC complex. Upon binding to damaged DNA, the Cullin 4 ubiquitin ligase associated with DDB1-DDB2 is activated and ubiquitinates DDB2 and XPC. The structurally disordered N-terminal tail of DDB2 contains seven lysines identified as major sites for ubiquitination that target the protein for proteasomal degradation; however, the precise biological functions of these modifications remained unknown. By exogenous expression of mutant DDB2 proteins in normal human fibroblasts, here we show that the N-terminal tail of DDB2 is involved in regulation of cellular responses to UV. By striking contrast with behaviors of exogenous DDB2, the endogenous DDB2 protein was stabilized even after UV irradiation as a function of the XPC expression level. Furthermore, XPC competitively suppressed ubiquitination of DDB2 in vitro, and this effect was significantly promoted by centrin-2, which augments the DNA damage-recognition activity of XPC. Based on these findings, we propose that in cells exposed to UV, DDB2 is protected by XPC from ubiquitination and degradation in a stochastic manner; thus XPC allows DDB2 to initiate multiple rounds of repair events, thereby contributing to the persistence of cellular DNA repair capacity.
    Feb. 2015, Nucleic acids research, 43(3) (3), 1700 - 13, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • AKITA Masaki, SUGASAWA Kaoru
    For organisms, a fundamental problem is how the huge genome can be searched appropriately for DNA damage in order to prevent genome instability and/or cell death. In mammalian nucleotide excision repair (NER), this process involves multiple protein factors containing the xeroderma pigmentosum gene products (UV-DDB, XPC, TFIIH), which sense different aspects of DNA structural abnormalities, respectively. Coordinated stepwise actions of these factors contribute to simultaneous achievement of versatility, efficiency and accuracy of the DNA quality control for NER.
    The Biophysical Society of Japan General Incorporated Association, 2015, Seibutsu Butsuri, 55(3) (3), 137 - 141, Japanese

  • Wataru Sakai, Kaoru Sugasawa
    Elsevier, Oct. 2014, FEBS Letters, 588(20) (20), 3778 - 3785, English
    [Refereed]
    Scientific journal

  • Wataru Sakai, Kaoru Sugasawa
    Oct. 2014, FEBS LETTERS, 588(20) (20), 3778 - 3785, English
    [Refereed]
    Scientific journal

  • Tatsuya Toga, Isao Kuraoka, Shun Watanabe, Eiji Nakano, Seiji Takeuchi, Chikako Nishigori, Kaoru Sugasawa, Shigenori Iwai
    Jul. 2014, SCIENTIFIC REPORTS, 4, 5578, English
    [Refereed]
    Scientific journal

  • Tatsuya Toga, Isao Kuraoka, Shun Watanabe, Eiji Nakano, Seiji Takeuchi, Chikako Nishigori, Kaoru Sugasawa, Shigenori Iwai
    Jul. 2014, SCIENTIFIC REPORTS, 4, 5578, English
    [Refereed]
    Scientific journal

  • Taishi Moriyama, Yuka Fujimitsu, Yushi Yoshikai, Takashi Sasano, Koji Yamada, Masataka Murakami, Takeshi Urano, Kaoru Sugasawa, Hisato Saitoh
    May 2014, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 447(3) (3), 419 - 424, English
    [Refereed]
    Scientific journal

  • Junya Unno, Akiko Itaya, Masato Taoka, Koichi Sato, Junya Tomida, Wataru Sakai, Kaoru Sugasawa, Masamichi Ishiai, Tsuyoshi Ikura, Toshiaki Isobe, Hitoshi Kurumizaka, Minoru Takata
    May 2014, CELL REPORTS, 7(4) (4), 1039 - 1047, English
    [Refereed]
    Scientific journal

  • Taishi Moriyama, Yuka Fujimitsu, Yushi Yoshikai, Takashi Sasano, Koji Yamada, Masataka Murakami, Takeshi Urano, Kaoru Sugasawa, Hisato Saitoh
    May 2014, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 447(3) (3), 419 - 424, English
    [Refereed]
    Scientific journal

  • Junya Unno, Akiko Itaya, Masato Taoka, Koichi Sato, Junya Tomida, Wataru Sakai, Kaoru Sugasawa, Masamichi Ishiai, Tsuyoshi Ikura, Toshiaki Isobe, Hitoshi Kurumizaka, Minoru Takata
    May 2014, CELL REPORTS, 7(4) (4), 1039 - 1047, English
    [Refereed]
    Scientific journal

  • Yokota Hiroaki, Tone Daisuke, Han Yong-Woon, Harada Yoshie, Sugasawa Kaoru
    The Biophysical Society of Japan General Incorporated Association, 2014, Seibutsu Butsuri, 54(1) (1), S214, English

  • Naoki Okashita, Yuichi Kumaki, Kuniaki Ebi, Miyuki Nishi, Yoshinori Okamoto, Megumi Nakayama, Shota Hashimoto, Tomohumi Nakamura, Kaoru Sugasawa, Nakao Kojima, Tatsuyuki Takada, Masaki Okano, Yoshiyuki Seki
    Jan. 2014, DEVELOPMENT, 141(2) (2), 269 - 280, English
    [Refereed]
    Scientific journal

  • Human mediator MED17 subunit plays essential roles in gene regulation by associating with the transcription and DNA repair machineries.
    Kikuchi, Y, Umemura, H, Nishitani, S, Iida, S, Fukasawa, R, Hayashi, H, Hirose, Y, Tanaka, A, Sugasawa, K, Ohkuma, Y
    2014, Genes Cells., 20(3) (3), 191 - 202, English
    [Refereed]
    Scientific journal

  • Naoki Okashita, Yuichi Kumaki, Kuniaki Ebi, Miyuki Nishi, Yoshinori Okamoto, Megumi Nakayama, Shota Hashimoto, Tomohumi Nakamura, Kaoru Sugasawa, Nakao Kojima, Tatsuyuki Takada, Masaki Okano, Yoshiyuki Seki
    Jan. 2014, DEVELOPMENT, 141(2) (2), 269 - 280, English
    [Refereed]
    Scientific journal

  • Yuliya S. Krasikova, Nadejda I. Rechkunova, Ekaterina A. Maltseva, Rashid O. Anarbaev, Pavel E. Pestryakov, Kaoru Sugasawa, Jung-Hyun Min, Olga I. Lavrik
    Dec. 2013, Journal of Molecular Recognition, 26(12) (12), 653 - 661, English
    [Refereed]
    Scientific journal

  • Ryotaro Nishi, Wataru Sakai, Daisuke Tone, Fumio Hanaoka, Kaoru Sugasawa
    Centrin-2 is an evolutionarily conserved, calmodulin-related protein, which is involved in multiple cellular functions including centrosome regulation and nucleotide excision repair (NER) of DNA. Particularly to exert the latter function, complex formation with the XPC protein, the pivotal NER damage recognition factor, is crucial. Here, we show that the C-terminal half of centrin-2, containing two calcium-binding EF-hand motifs, is necessary and sufficient for both its localization to the centrosome and interaction with XPC. In XPC-deficient cells, nuclear localization of overexpressed centrin-2 largely depends on co-overexpression of XPC, and mutational analyses of the C-terminal domain suggest that XPC and the major binding partner in the centrosome share a common binding surface on the centrin-2 molecule. On the other hand, the N-terminal domain of centrin-2 also contains two EF-hand motifs but shows only low-binding affinity for calcium ions. Although the N-terminal domain is dispensable for enhancement of the DNA damage recognition activity of XPC, it contributes to augmenting rather weak physical interaction between XPC and XPA, another key factor involved in NER. These results suggest that centrin-2 may have evolved to bridge two protein factors, one with high affinity and the other with low affinity, thereby allowing delicate regulation of various biological processes.
    Aug. 2013, Nucleic acids research, 41(14) (14), 6917 - 29, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Koji Kikuchi, Takeo Narita, Van T. Pham, Junko Iijima, Kouji Hirota, Islam Shamima Keka, Katsuya Okawa, Tetsuya Hori, Tatsuo Fukagawa, Jeroen Essers, Roland Kanaar, Matthew C. Whitby, Kaoru Sugasawa, Yoshihito Taniguchi, Katsumi Kitagawa, Shunichi Takeda
    Jul. 2013, CANCER RESEARCH, 73(14) (14), 4362 - 4371, English
    [Refereed]
    Scientific journal

  • Structure-function analysis of the EF-hand protein centrin-2 for its intracellular localization and nucleotide excision repair.
    Nishi, R, Sakai, W, Tone, D, Hanaoka, F, SUGASAWA KAORU
    May 2013, Nucleic Acids Res, English
    [Refereed]
    Scientific journal

  • Kikuchi, K, Narita, T, Pham, VT, Iijima, J, Hirota, K, Keka, IS, Mohiuddin, M, Okawa, K, Hori, T, Fukagawa, T, Essers, J, Kanaar, R, Whitby, MC, SUGASAWA KAORU, Taniguchi, Y, Kitagawa, K, Takeda, S
    DNA double-strand breaks (DSB) occur frequently during replication in sister chromatids and are dramatically increased when cells are exposed to chemotherapeutic agents including camptothecin. Such DSBs are efficiently repaired specifically by homologous recombination (HR) with the intact sister chromatid. HR, therefore, plays pivotal roles in cellular proliferation and cellular tolerance to camptothecin. Mammalian cells carry several structure-specific endonucleases, such as Xpf-Ercc1 and Mus81-Eme1, in which Xpf and Mus81 are the essential subunits for enzymatic activity. Here, we show the functional overlap between Xpf and Mus81 by conditionally inactivating Xpf in the chicken DT40 cell line, which has no Mus81 ortholog. Although mammalian cells deficient in either Xpf or Mus81 are viable, Xpf inactivation in DT40 cells was lethal, resulting in a marked increase in the number of spontaneous chromosome breaks. Similarly, inactivation of both Xpf and Mus81 in human HeLa cells and murine embryonic stem cells caused numerous spontaneous chromosome breaks. Furthermore, the phenotype of Xpf-deficient DT40 cells was reversed by ectopic expression of human Mus81-Eme1 or human Xpf-Ercc1 heterodimers. These observations indicate the functional overlap of Xpf-Ercc1 and Mus81-Eme1 in the maintenance of genomic DNA. Both Mus81-Eme1 and Xpf-Ercc1 contribute to the completion of HR, as evidenced by the data that the expression of Mus81-Eme1 or Xpf-Ercc1 diminished the number of camptothecin-induced chromosome breaks in Xpf-deficient DT40 cells, and to preventing early steps in HR by deleting XRCC3 suppressed the nonviability of Xpf-deficient DT40 cells. In summary, Xpf and Mus81 have a substantially overlapping function in completion of HR.
    Apr. 2013, Cancer Res, 73(14) (14), 4362 - 71, English, International magazine
    [Refereed]
    Scientific journal

  • Yuliya S. Krasikova, Nadejda I. Rechkunova, Ekaterina A. Maltseva, Pavel E. Pestryakov, Irina O. Petruseva, Kaoru Sugasawa, Xuejing Chen, Jung-Hyun Min, Olga I. Lavrik
    Apr. 2013, JOURNAL OF BIOLOGICAL CHEMISTRY, 288(15) (15), 10936 - 10947, English
    [Refereed]
    Scientific journal

  • Yuliya S. Krasikova, Nadejda I. Rechkunova, Ekaterina A. Maltseva, Pavel E. Pestryakov, Irina O. Petruseva, Kaoru Sugasawa, Xuejing Chen, Jung-Hyun Min, Olga I. Lavrik
    Apr. 2013, JOURNAL OF BIOLOGICAL CHEMISTRY, 288(15) (15), 10936 - 10947, English
    [Refereed]
    Scientific journal

  • Yokota Hiroaki, Tone Daisuke, Han Yong-Woon, Harada Yoshie, Sugasawa Kaoru
    The Biophysical Society of Japan General Incorporated Association, 2013, Seibutsu Butsuri, 53(1) (1), S178, Japanese

  • Identification of new acetylated proteins involved in DNA damage response
    Takeshi Yasuda, Kengo Saito, Wataru Kagawa, Tomoo Ogi, Takehiro Suzuki, Naoshi Dohmae, Takuya Hino, Yuka Nakazawa, Ai Nakamura, Masaharu Hazawa, Fumio Hanaoka, Kaoru Sugasawa, Ryuichi Okayasu, Hitoshi Kurumizaka, Katsushi Tajima
    Dec. 2012, GENES & GENETIC SYSTEMS, 87(6) (6), 411 - 411, English
    [Refereed]

  • Alex Pines, Mischa G. Vrouwe, Jurgen A. Marteijn, Dimitris Typas, Martijn S. Luijsterburg, Medine Cansoy, Paul Hensbergen, Andre Deelder, Anton de Groot, Syota Matsumoto, Kaoru Sugasawa, Nicolas Thoma, Wim Vermeulen, Harry Vrieling, Leon Mullenders
    Oct. 2012, JOURNAL OF CELL BIOLOGY, 199(2) (2), 235 - 249, English
    [Refereed]
    Scientific journal

  • Yasushi Shiomi, Akiyo Hayashi, Takashi Ishii, Kaori Shinmyozu, Jun-ichi Nakayama, Kaoru Sugasawa, Hideo Nishitani
    Jun. 2012, MOLECULAR AND CELLULAR BIOLOGY, 32(12) (12), 2279 - 2288, English
    [Refereed]
    Scientific journal

  • Two different replication factor C proteins, Ctf18 and RFC1, separately control
    Shiomi, Y, Hayashi, A, Ishii, T, Shinmyozu, K, Nakayama, J. I, Sugasawa, K, Nishitani, H
    Jun. 2012, Mol Cell Biol, 32巻、12号、2279-2288頁, English
    Scientific journal

  • Eric S Fischer, Andrea Scrima, Kerstin Böhm, Syota Matsumoto, Gondichatnahalli M Lingaraju, Mahamadou Faty, Takeshi Yasuda, Simone Cavadini, Mitsuo Wakasugi, Fumio Hanaoka, Shigenori Iwai, Heinz Gut, Kaoru Sugasawa, Nicolas H Thomä
    The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). The DCAF DDB2 detects UV-induced pyrimidine dimers in the genome and facilitates nucleotide excision repair. We provide the molecular basis for DDB2 receptor-mediated cyclobutane pyrimidine dimer recognition in chromatin. The structures of the fully assembled DDB1-DDB2-CUL4A/B-RBX1 (CRL4(DDB2)) ligases reveal that the mobility of the ligase arm creates a defined ubiquitination zone around the damage, which precludes direct ligase activation by DNA lesions. Instead, the COP9 signalosome (CSN) mediates the CRL4(DDB2) inhibition in a CSN5 independent, nonenzymatic, fashion. In turn, CSN inhibition is relieved upon DNA damage binding to the DDB2 module within CSN-CRL4(DDB2). The Cockayne syndrome A DCAF complex crystal structure shows that CRL4(DCAF(WD40)) ligases share common architectural features. Our data support a general mechanism of ligase activation, which is induced by CSN displacement from CRL4(DCAF) on substrate binding to the DCAF.
    Nov. 2011, Cell, 147(5) (5), 1024 - 39, English, International magazine
    [Refereed]
    Scientific journal

  • DNA damage recognition for mammalian global genome nucleotide excision repair.
    Sugasawa, K
    Nov. 2011, DNA Repair (ed. Kruman, I.), 453-476, English
    Scientific journal

  • Hiromi Yanagihara, Junya Kobayashi, Satoshi Tateishi, Akihiro Kato, Shinya Matsuura, Hiroshi Tauchi, Kouichi Yamada, Jun Takezawa, Kaoru Sugasawa, Chikahide Masutani, Fumio Hanaoka, Corry M Weemaes, Toshio Mori, Lee Zou, Kenshi Komatsu
    Translesion DNA synthesis, a process orchestrated by monoubiquitinated PCNA, is critical for DNA damage tolerance. While the ubiquitin-conjugating enzyme RAD6 and ubiquitin ligase RAD18 are known to monoubiquitinate PCNA, how they are regulated by DNA damage is not fully understood. We show that NBS1 (mutated in Nijmegen breakage syndrome) binds to RAD18 after UV irradiation and mediates the recruitment of RAD18 to sites of DNA damage. Disruption of NBS1 abolished RAD18-dependent PCNA ubiquitination and Polη focus formation, leading to elevated UV sensitivity and mutation. Unexpectedly, the RAD18-interacting domain of NBS1, which was mapped to its C terminus, shares structural and functional similarity with the RAD18-interacting domain of RAD6. These domains of NBS1 and RAD6 allow the two proteins to interact with RAD18 homodimers simultaneously and are crucial for Polη-dependent UV tolerance. Thus, in addition to chromosomal break repair, NBS1 plays a key role in translesion DNA synthesis.
    Sep. 2011, Molecular cell, 43(5) (5), 788 - 97, English, International magazine
    [Refereed]
    Scientific journal

  • Hiromi Yanagihara, Junya Kobayashi, Satoshi Tateishi, Akihiro Kato, Shinya Matsuura, Hiroshi Tauchi, Kouichi Yamada, Jun Takezawa, Kaoru Sugasawa, Chikahide Masutani, Fumio Hanaoka, Corry M Weemaes, Toshio Mori, Lee Zou, Kenshi Komatsu
    Translesion DNA synthesis, a process orchestrated by monoubiquitinated PCNA, is critical for DNA damage tolerance. While the ubiquitin-conjugating enzyme RAD6 and ubiquitin ligase RAD18 are known to monoubiquitinate PCNA, how they are regulated by DNA damage is not fully understood. We show that NBS1 (mutated in Nijmegen breakage syndrome) binds to RAD18 after UV irradiation and mediates the recruitment of RAD18 to sites of DNA damage. Disruption of NBS1 abolished RAD18-dependent PCNA ubiquitination and Polη focus formation, leading to elevated UV sensitivity and mutation. Unexpectedly, the RAD18-interacting domain of NBS1, which was mapped to its C terminus, shares structural and functional similarity with the RAD18-interacting domain of RAD6. These domains of NBS1 and RAD6 allow the two proteins to interact with RAD18 homodimers simultaneously and are crucial for Polη-dependent UV tolerance. Thus, in addition to chromosomal break repair, NBS1 plays a key role in translesion DNA synthesis.
    Sep. 2011, Molecular cell, 43(5) (5), 788 - 97, English, International magazine
    [Refereed]
    Scientific journal

  • Hanspeter Naegeli, Kaoru Sugasawa
    Jul. 2011, DNA REPAIR, 10(7) (7), 673 - 683, English
    [Refereed]
    Scientific journal

  • Fumio Yatagai, Masamitsu Honma, Akihisa Takahashi, Katsunori Omori, Hiromi Suzuki, Toru Shimazu, Masaya Seki, Toko Hashizume, Akiko Ukai, Kaoru Sugasawa, Tomoko Abe, Naoshi Dohmae, Shuichi Enomoto, Takeo Ohnishi, Alasdair Gordon, Noriaki Ishioka
    Mar. 2011, RADIATION AND ENVIRONMENTAL BIOPHYSICS, 50(1) (1), 125 - 134, English
    [Refereed]
    Scientific journal

  • Multiple DNA damage recognition factors involved in mammalian nucleotide excision repair
    SUGASAWA Kaoru
    Jan. 2011, Biochemistry, 76: 16-23, English
    [Refereed]
    Scientific journal

  • Niina Tanaka, Miki Goto, Azusa Kawasaki, Takashi Sasano, Ko Eto, Ryotaro Nishi, Kaoru Sugasawa, Shinichi Abe, Hisato Saitoh
    Oct. 2010, CELL BIOCHEMISTRY AND FUNCTION, 28(7) (7), 604 - 612, English
    [Refereed]
    Scientific journal

  • Yuichiro Shimizu, Yasuhiro Uchimura, Naoshi Dohmae, Hisato Saitoh, Fumio Hanaoka, Kaoru Sugasawa
    We showed that XPC complex, which is a DNA damage detector for nucleotide excision repair, stimulates activity of thymine DNA glycosylase (TDG) that initiates base excision repair. XPC appeared to facilitate the enzymatic turnover of TDG by promoting displacement from its own product abasic site, although the precise mechanism underlying this stimulation has not been clarified. Here we show that XPC has only marginal effects on the activity of E. coli TDG homolog (EcMUG), which remains bound to the abasic site like human TDG but does not significantly interacts with XPC. On the contrary, XPC significantly stimulates the activities of sumoylated TDG and SMUG1, both of which exhibit quite different enzymatic kinetics from unmodified TDG but interact with XPC. These results point to importance of physical interactions for stimulation of DNA glycosylases by XPC and have implications in the molecular mechanisms underlying mutagenesis and carcinogenesis in XP-C patients.
    Jul. 2010, Journal of nucleic acids, 2010, English, International magazine
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Naoyuki Matsumoto, Tatsuya Toga, Ryosuke Hayashi, Kaoru Sugasawa, Katsuo Katayanagi, Hiroshi Ide, Isao Kuraoka, Shigenori Iwai
    Apr. 2010, NUCLEIC ACIDS RESEARCH, 38(7) (7), English
    [Refereed]
    Scientific journal

  • Naoyuki Matsumoto, Tatsuya Toga, Ryosuke Hayashi, Kaoru Sugasawa, Katsuo Katayanagi, Hiroshi Ide, Isao Kuraoka, Shigenori Iwai
    Jan. 2010, Nucleic Acids Research, 38(7) (7), e101, English
    Scientific journal

  • Kaoru Sugasawa, Jun-ichi Akagi, Ryotaro Nishi, Shigenori Iwai, Fumio Hanaoka
    For mammalian nucleotide excision repair (NER), DNA lesions are recognized in at least two steps involving detection of unpaired bases by the XPC protein complex and the subsequent verification of injured bases. Although lesion verification is important to ensure high damage discrimination and the accuracy of the repair system, it has been unclear how this is accomplished. Here, we show that damage verification involves scanning of a DNA strand from the site where XPC is initially bound. Translocation by the NER machinery exhibits a 5'-to-3' directionality, strongly suggesting involvement of the XPD helicase, a component of TFIIH. Furthermore, the initial orientation of XPC binding is crucial in that only one DNA strand is selected to search for the presence of lesions. Our results dissect the intricate molecular mechanism of NER and provide insights into a strategy for mammalian cells to survey large genomes to detect DNA damage.
    Nov. 2009, Molecular cell, 36(4) (4), 642 - 53, English, International magazine
    [Refereed]
    Scientific journal

  • Katsuhito Kino, Kaoru Sugasawa, Takeshi Mizuno, Toshikazu Bando, Hiroshi Sugiyama, Masaki Akita, Hiroshi Miyazawa, Fumio Hanaoka
    Nov. 2009, Chembiochem : a European journal of chemical biology, 10(16) (16), 2613 - 6, English, International magazine
    [Refereed]
    Scientific journal

  • Ryotaro Nishi, Sergey Alekseev, Christoffel Dinant, Deborah Hoogstraten, Adriaan B Houtsmuller, Jan H J Hoeijmakers, Wim Vermeulen, Fumio Hanaoka, Kaoru Sugasawa
    Although the basic principle of nucleotide excision repair (NER), which can eliminate various DNA lesions, have been dissected at the genetic, biochemical and cellular levels, the important in vivo regulation of the critical damage recognition step is poorly understood. Here we analyze the in vivo dynamics of the essential NER damage recognition factor XPC fused to the green fluorescence protein (GFP). Fluorescence recovery after photobleaching analysis revealed that the UV-induced transient immobilization of XPC, reflecting its actual engagement in NER, is regulated in a biphasic manner depending on the number of (6-4) photoproducts and titrated by the number of functional UV-DDB molecules. A similar biphasic UV-induced immobilization of TFIIH was observed using XPB-GFP. Surprisingly, subsequent integration of XPA into the NER complex appears to follow only the low UV dose immobilization of XPC. Our results indicate that when only a small number of (6-4) photoproducts are generated, the UV-DDB-dependent damage recognition pathway predominates over direct recognition by XPC, and they also suggest the presence of rate-limiting regulatory steps in NER prior to the assembly of XPA.
    Jun. 2009, DNA repair, 8(6) (6), 767 - 76, English, International magazine
    Scientific journal

  • Ryotaro Nishi, Sergey Alekseev, Christoffel Dinant, Deborah Hoogstraten, Adriaan B Houtsmuller, Jan H J Hoeijmakers, Wim Vermeulen, Fumio Hanaoka, Kaoru Sugasawa
    Although the basic principle of nucleotide excision repair (NER), which can eliminate various DNA lesions, have been dissected at the genetic, biochemical and cellular levels, the important in vivo regulation of the critical damage recognition step is poorly understood. Here we analyze the in vivo dynamics of the essential NER damage recognition factor XPC fused to the green fluorescence protein (GFP). Fluorescence recovery after photobleaching analysis revealed that the UV-induced transient immobilization of XPC, reflecting its actual engagement in NER, is regulated in a biphasic manner depending on the number of (6-4) photoproducts and titrated by the number of functional UV-DDB molecules. A similar biphasic UV-induced immobilization of TFIIH was observed using XPB-GFP. Surprisingly, subsequent integration of XPA into the NER complex appears to follow only the low UV dose immobilization of XPC. Our results indicate that when only a small number of (6-4) photoproducts are generated, the UV-DDB-dependent damage recognition pathway predominates over direct recognition by XPC, and they also suggest the presence of rate-limiting regulatory steps in NER prior to the assembly of XPA.
    Jun. 2009, DNA repair, 8(6) (6), 767 - 76, English, International magazine
    [Refereed]
    Scientific journal

  • Regulation of damage recognition in mammalian global genomic nucleotide excision repair
    SUGASAWA Kaoru
    Mar. 2009, Mutat. Res., 685: 19-37, English
    [Refereed]
    Scientific journal

  • Y. Roche, D. Zhang, G. M. J. Segers-Nolten, W. Vermeulen, C. Wyman, K. Sugasawa, J. Hoeijmakers, C. Otto
    Sep. 2008, JOURNAL OF FLUORESCENCE, 18(5) (5), 987 - 995, English
    [Refereed]
    Scientific journal

  • Y. Roche, D. Zhang, G. M J Segers-Nolten, W. Vermeulen, C. Wyman, K. Sugasawa, J. Hoeijmakers, C. Otto
    Sep. 2008, Journal of Fluorescence, 18(5) (5), 987 - 995, English
    Scientific journal

  • Kaoru Sugasawa
    Mar. 2008, Carcinogenesis, 29(3) (3), 455 - 465, English
    [Refereed]
    Scientific journal
    Link to Kobe Univ. Repository (Kernel)

  • Mutagenic radioadaptation in a human lymphoblastoid cell line.
    Fumio Yatagai, Yukihiro Umebayashi, Masamitsu Honma, Kaoru Sugasawa, Yuko Takayama, Fumio Hanaoka
    We investigated the mutagenic radioadaptive response of human lymphoblastoid TK6 cells by pretreating them with a low dose (5 cGy) of X-rays followed by a high (2 Gy) dose 6h later. Pretreatment reduced the 2-Gy-induced mutation frequency (MF) of the thymidine kinase (TK) gene (18.3 x 10(-6)) to 62% of the original level (11.4 x 10(-6)). A loss of heterozygosity (LOH) detection analysis applied to the isolated TK(-) mutants revealed the mutational events as non-LOH (resulting mostly from a point mutation in the TK gene), hemizygous LOH (resulting from a chromosomal deletion), or homozygous LOH (resulting from homologous recombination (HR) between chromosomes). For non-LOH events, pretreatment decreased the frequency to 27% of the original level (from 7.1 x 10(-6) to 1.9 x 10(-6)). cDNAs prepared from the non-LOH mutants revealed that the decrease was due mainly to the repression of base substitutions. The frequency of hemizygous LOH events, however, was not significantly altered by pretreatment. Mapping analysis of chromosome 17 demonstrated that the distribution and the extent of hemizygous LOH events were also not significantly influenced by pretreatment. For homozygous LOH events, pretreatment reduced the frequency to 61% of the original level (from 5.1 x 10(-6) to 3.1 x 10(-6)), reflecting an enhancement in HR repair of DNA double-strand breaks. Our findings suggest that the radioadaptive response in TK6 cells follows mainly from mutations at the base-sequence level, not the chromosome level.
    Feb. 2008, Mutation research, 638(1-2) (1-2), 48 - 55, English, International magazine
    [Refereed]
    Scientific journal

  • In vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation.
    Gentaro Yasuda, Ryotaro Nishi, Eriko Watanabe, Toshio Mori, Shigenori Iwai, Donata Orioli, Miria Stefanini, Fumio Hanaoka, Kaoru Sugasawa
    Xeroderma pigmentosum group C (XPC) protein plays an essential role in DNA damage recognition in mammalian global genome nucleotide excision repair (NER). Here, we analyze the functional basis of NER inactivation caused by a single amino acid substitution (Trp to Ser at position 690) in XPC, previously identified in the XPC patient XP13PV. The Trp690Ser change dramatically affects the in vivo stability of the XPC protein, thereby causing a significant reduction of its steady-state level in XP13PV fibroblasts. Despite normal heterotrimeric complex formation and physical interactions with other NER factors, the mutant XPC protein lacks binding affinity for both undamaged and damaged DNA. Thus, this single amino acid substitution is sufficient to compromise XPC function through both quantitative and qualitative alterations of the protein. Although the mutant XPC fails to recognize damaged DNA, it is still capable of accumulating in a UV-damaged DNA-binding protein (UV-DDB)-dependent manner to UV-damaged subnuclear domains. However, the NER factors transcription factor IIH and XPA failed to colocalize stably with the mutant XPC. As well as highlighting the importance of UV-DDB in recruiting XPC to UV-damaged sites, these findings demonstrate the role of DNA binding by XPC in the assembly of subsequent NER intermediate complexes.
    Oct. 2007, Molecular and cellular biology, 27(19) (19), 6606 - 14, English, International magazine
    [Refereed]
    Scientific journal

  • [Roles for ubiquitylation in DNA repair].
    Kaoru Sugasawa, Fumio Hanaoka
    Jun. 2007, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 52(7) (7), 760 - 7, Japanese, Domestic magazine
    Scientific journal

  • 紫外線によるDNA損傷の修復機構
    西 良太郎, 菅澤 薫
    共立出版, Nov. 2006, 蛋白質核酸酵素, 51(14) (14), 2126-2133 - 2133,1919, Japanese

  • Steven Bergink, Lies-Anne Severijnen, Nils Wijgers, Kaoru Sugasawa, Humaira Yousaf, Johan M. Kros, John van Swieten, Ben A. Oostra, Jan H. Hoeijmakers, Wim Vermeulen, Rob Willemsen
    Sep. 2006, NEUROBIOLOGY OF DISEASE, 23(3) (3), 708 - 716, English
    [Refereed]
    Scientific journal

  • [Repair mechanism of DNA base lesions induced by ultraviolet light irradiation].
    Kaoru Sugasawa, Fumio Hanaoka
    Jun. 2006, Seikagaku. The Journal of Japanese Biochemical Society, 78(6) (6), 516 - 21, Japanese, Domestic magazine
    [Refereed]

  • Daichi Baba, Nobuo Maita, Jun-Goo Jee, Yasuhiro Uchimura, Hisato Saitoh, Kaoru Sugasawa, Fumio Hanaoka, Hidehito Tochio, Hidekazu Hiroaki, Masahiro Shirakawa
    Modification of cellular proteins by the small ubiquitin-like modifier SUMO is important in regulating various cellular events. Many different nuclear proteins are targeted by SUMO, and the functional consequences of this modification are diverse. For most proteins, however, the functional and structural consequences of modification by specific SUMO isomers are unclear. Conjugation of SUMO to thymine-DNA glycosylase (TDG) induces the dissociation of TDG from its product DNA. Structure determination of the TDG central region conjugated to SUMO-1 previously suggested a mechanism in which the SUMOylation-induced conformational change in the C-terminal region of TDG releases TDG from tight binding to its product DNA. Here, we have determined the crystal structure of the central region of TDG conjugated to SUMO-3. The overall structure of SUMO-3-conjugated TDG is similar to the previously reported structure of TDG conjugated to SUMO-1, despite the relatively low level of amino acid sequence similarity between SUMO-3 and SUMO-1. The two structures revealed that the sequence of TDG that resembles the SUMO-binding motif (SBM) can form an intermolecular beta-sheet with either SUMO-1 or SUMO-3. Structural comparison with the canonical SBM shows that this SBM-like sequence of TDG retains all of the characteristic interactions of the SBM, indicating sequence diversity in the SBM.
    May 2006, Journal of molecular biology, 359(1) (1), 137 - 47, English, International magazine
    [Refereed]
    Scientific journal

  • Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.
    Ryotaro Nishi, Yuki Okuda, Eriko Watanabe, Toshio Mori, Shigenori Iwai, Chikahide Masutani, Kaoru Sugasawa, Fumio Hanaoka
    Xeroderma pigmentosum group C (XPC) protein plays a key role in DNA damage recognition in global genome nucleotide excision repair (NER). The protein forms in vivo a heterotrimeric complex involving one of the two human homologs of Saccharomyces cerevisiae Rad23p and centrin 2, a centrosomal protein. Because centrin 2 is dispensable for the cell-free NER reaction, its role in NER has been unclear. Binding experiments with a series of truncated XPC proteins allowed the centrin 2 binding domain to be mapped to a presumed alpha-helical region near the C terminus, and three amino acid substitutions in this domain abrogated interaction with centrin 2. Human cell lines stably expressing the mutant XPC protein exhibited a significant reduction in global genome NER activity. Furthermore, centrin 2 enhanced the cell-free NER dual incision and damaged DNA binding activities of XPC, which likely require physical interaction between XPC and centrin 2. These results reveal a novel vital function for centrin 2 in NER, the potentiation of damage recognition by XPC.
    Jul. 2005, Molecular and cellular biology, 25(13) (13), 5664 - 74, English, International magazine
    [Refereed]

  • Signal transducer and activator of transcription 3 is a key regulator of keratinocyte survival and proliferation following UV irradiation
    S Sano, KS Chan, M Kira, K Kataoka, S Takagi, M Tarutani, S Itami, K Kiguchi, M Yokoi, K Sugasawa, T Mori, F Hanaoka, J Takeda, J DiGiovanni
    Jul. 2005, CANCER RESEARCH, 65(13) (13), 5720 - 5729, English
    [Refereed]
    Scientific journal

  • Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.
    Daichi Baba, Nobuo Maita, Jun-Goo Jee, Yasuhiro Uchimura, Hisato Saitoh, Kaoru Sugasawa, Fumio Hanaoka, Hidehito Tochio, Hidekazu Hiroaki, Masahiro Shirakawa
    Members of the small ubiquitin-like modifier (SUMO) family can be covalently attached to the lysine residue of a target protein through an enzymatic pathway similar to that used in ubiquitin conjugation, and are involved in various cellular events that do not rely on degradative signalling via the proteasome or lysosome. However, little is known about the molecular mechanisms of SUMO-modification-induced protein functional transfer. During DNA mismatch repair, SUMO conjugation of the uracil/thymine DNA glycosylase TDG promotes the release of TDG from the abasic (AP) site created after base excision, and coordinates its transfer to AP endonuclease 1, which catalyses the next step in the repair pathway. Here we report the crystal structure of the central region of human TDG conjugated to SUMO-1 at 2.1 A resolution. The structure reveals a helix protruding from the protein surface, which presumably interferes with the product DNA and thus promotes the dissociation of TDG from the DNA molecule. This helix is formed by covalent and non-covalent contacts between TDG and SUMO-1. The non-covalent contacts are also essential for release from the product DNA, as verified by mutagenesis.
    Jun. 2005, Nature, 435(7044) (7044), 979 - 82, English, International magazine
    [Refereed]
    Scientific journal

  • UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex.
    Kaoru Sugasawa, Yuki Okuda, Masafumi Saijo, Ryotaro Nishi, Noriyuki Matsuda, Gilbert Chu, Toshio Mori, Shigenori Iwai, Keiji Tanaka, Kiyoji Tanaka, Fumio Hanaoka
    The xeroderma pigmentosum group C (XPC) protein complex plays a key role in recognizing DNA damage throughout the genome for mammalian nucleotide excision repair (NER). Ultraviolet light (UV)-damaged DNA binding protein (UV-DDB) is another complex that appears to be involved in the recognition of NER-inducing damage, although the precise role it plays and its relationship to XPC remain to be elucidated. Here we show that XPC undergoes reversible ubiquitylation upon UV irradiation of cells and that this depends on the presence of functional UV-DDB activity. XPC and UV-DDB were demonstrated to interact physically, and both are polyubiquitylated by the recombinant UV-DDB-ubiquitin ligase complex. The polyubiquitylation altered the DNA binding properties of XPC and UV-DDB and appeared to be required for cell-free NER of UV-induced (6-4) photoproducts specifically when UV-DDB was bound to the lesion. Our results strongly suggest that ubiquitylation plays a critical role in the transfer of the UV-induced lesion from UV-DDB to XPC.
    May 2005, Cell, 121(3) (3), 387 - 400, English, International magazine
    [Refereed]

  • Nucleosomal structure of undamaged DNA regions suppresses the non-specific DNA binding of the XPC complex.
    Takeshi Yasuda, Kaoru Sugasawa, Yuichiro Shimizu, Shigenori Iwai, Tadahiro Shiomi, Fumio Hanaoka
    The XPC protein complex is a DNA damage detector of human nucleotide excision repair (NER). Although the XPC complex specifically binds to certain damaged sites, it also binds to undamaged DNA in a non-specific manner. The addition of a large excess of undamaged naked DNA competitively inhibited the specific binding of the XPC complex to (6-4) photoproducts and the NER dual incision step in cell-free extracts. In contrast, the addition of undamaged nucleosomal DNA as a competitor suppressed both of these inhibitory effects. Although nucleosomes positioned on the damaged site inhibited the binding of the XPC complex, the presence of nucleosomes in undamaged DNA regions may help specific binding of the XPC complex to damaged sites by excluding its non-specific binding to undamaged DNA regions.
    Mar. 2005, DNA repair, 4(3) (3), 389 - 95, English, International magazine
    [Refereed]

  • Shirakawa M., Baba D., Maita N., Saito H., Uchimura Y., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H.
    The Biophysical Society of Japan General Incorporated Association, 2005, Seibutsu Butsuri, 45, S9, English

  • Relative levels of the two mammalian Rad23 homologs determine composition and stability of the xeroderma pigmentosum group C protein complex.
    Yuki Okuda, Ryotaro Nishi, Jessica M Y Ng, Wim Vermeulen, Gijsbertus T J van der Horst, Toshio Mori, Jan H J Hoeijmakers, Fumio Hanaoka, Kaoru Sugasawa
    Mammalian cells express two Rad23 homologs, HR23A and HR23B, which have been implicated in regulation of proteolysis via the ubiquitin/proteasome pathway. Recently, the proteins have been shown to stabilize xeroderma pigmentosum group C (XPC) protein that is involved in DNA damage recognition for nucleotide excision repair (NER). Because the vast majority of XPC forms a complex with HR23B rather than HR23A, we investigated possible differences between the two Rad23 homologs in terms of their effects on the XPC protein. In wild-type mouse embryonic fibroblasts (MEFs), endogenous XPC was found to be relatively stable, while its steady-state level and stability appeared significantly reduced by targeted disruption of the mHR23B gene, but not by that of mHR23A. Loss of both mHR23 genes caused a strong further reduction of the XPC protein level. Quantification of the two mHR23 proteins revealed that in normal cells mHR23B is actually approximately 10 times more abundant than mHR23A. In addition, overexpression of mHR23A in the mHR23A/B double knock out cells restored not only the steady-state level and stability of the XPC protein, but also cellular NER activity to near wild-type levels. These results indicate that the two Rad23 homologs are largely functionally equivalent in NER, and that the difference in expression levels explains for a major part the difference in complex formation with as well as stabilization effects on XPC.
    Oct. 2004, DNA repair, 3(10) (10), 1285 - 95, English, International magazine
    [Refereed]

  • Yasuhiro Uchimura, Makoto Nakamura, Kaoru Sugasawa, Mitsuyoshi Nakao, Hisato Saitoh
    Aug. 2004, Analytical biochemistry, 331(1) (1), 204 - 6, English, International magazine
    Scientific journal

  • Nucleotide excision repair of 5-formyluracil in vitro is enhanced by the presence of mismatched bases.
    Katsuhito Kino, Yuichiro Shimizu, Kaoru Sugasawa, Hiroshi Sugiyama, Fumio Hanaoka
    5-Formyluracil (fU) is a major thymine lesion produced by reactive oxygen radicals and photosensitized oxidation. Although this residue is a potentially mutagenic lesion and is removed by several base excision repair enzymes, it is unknown whether fU is the substrate of nucleotide excision repair (NER). Here, we analyzed the binding specificity of XPC-HR23B, which initiates NER, and cell-free NER activity on fU opposite four different bases. The result of the gel mobility shift assay showed that XPC-HR23B binds the fU-containing substrates in the following order: fU:C > fU:T > fU:G > fU:A. Furthermore, in the presence of XPC-HR23B, the dual incision activity was the same as the order of the binding affinity of XPC-HR23B to fU. Therefore, it is concluded that even fU, regarded as a shape mimic of thymine, can be recognized as a substrate of NER incision, and the efficiency depends on instability of the base pair.
    Mar. 2004, Biochemistry, 43(10) (10), 2682 - 7, English, International magazine
    [Refereed]

  • Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B.
    Kenichiro Fujiwara, Takeshi Tenno, Kaoru Sugasawa, Jun-Goo Jee, Izuru Ohki, Chojiro Kojima, Hidehito Tochio, Hidekazu Hiroaki, Fumio Hanaoka, Masahiro Shirakawa
    Ubiquitination, a modification in which single or multiple ubiquitin molecules are attached to a protein, serves signaling functions that control several cellular processes. The ubiquitination signal is recognized by downstream effectors, many of which carry a ubiquitin-interacting motif (UIM). Such interactions can be modulated by regulators carrying a ubiquitin-like (UbL) domain, which binds UIM by mimicking ubiquitination. Of them, HR23B regulates the proteasomal targeting of ubiquitinated substrates, DNA repair factors, and other proteins. Here we report the structure of the UIM of the proteasome subunit S5a bound to the UbL domain of HR23B. The UbL domain presents one hydrophobic and two polar contact sites for interaction with UIM. The residues in these contact sites are well conserved in ubiquitin, but ubiquitin also presents a histidine at the interface. The pH-dependent protonation of this residue interferes with the access of ubiquitin to the UIM and the ubiquitin-associated domain (UBA), and its mutation to a smaller residue increases the affinity of ubiquitin for UIM.
    Feb. 2004, The Journal of biological chemistry, 279(6) (6), 4760 - 7, English, International magazine
    [Refereed]

  • Translesion synthesis by human DNA polymerase eta across oxidative products of guanine.
    Katuhito Kino, Nobutoshi Ito, Kaoru Sugasawa, Hiroshi Sugiyama, Fumio Hanaoka
    Guanine is the most oxidizable base among natural bases. 8-Oxoguanine (8-oxoG) is the typical oxidative product, but the amount of 8-oxoG does not directly reflect the strength of oxidative stress. Imidazolone, oxazolone and guanidinohydantoin are oxidative products of guanine and 8-oxoG. Here, we investigated enzymatic reactions with human DNA polymerase eta on these lesions.
    2004, Nucleic acids symposium series (2004), (48) (48), 171 - 2, English, International magazine
    [Refereed]

  • Thymine-rich single-stranded DNA activates Mcm4/6/7 helicase on Y-fork and bubble-like substrates.
    Zhiying You, Yukio Ishimi, Takeshi Mizuno, Kaoru Sugasawa, Fumio Hanaoka, Hisao Masai
    The presence of multiple clusters of runs of asymmetric adenine or thymine is a feature commonly found in eukaryotic replication origins. Here we report that the helicase and ATPase activities of the mammalian Mcm4/6/7 complex are activated specifically by thymine stretches. The Mcm helicase is specifically activated by a synthetic bubble structure which mimics an activated replication origin, as well as by a Y-fork structure, provided that a single-stranded DNA region of sufficient length is present in the unwound segment or 3' tail, respectively, and that it carries clusters of thymines. Sequences derived from the human lamin B2 origin can serve as a potent activator for the Mcm helicase, and substitution of its thymine clusters with guanine leads to loss of this activation. At the fork, Mcm displays marked processivity, expected for a replicative helicase. These findings lead us to propose that selective activation by stretches of thymine sequences of a fraction of Mcm helicases loaded onto chromatin may be the determinant for selection of initiation sites on mammalian genomes.
    Nov. 2003, The EMBO journal, 22(22) (22), 6148 - 60, English, International magazine
    [Refereed]

  • JMY Ng, W Vermeulen, GTJ van der Horst, S Bergink, K Sugasawa, H Vrieling, JHJ Hoeijmakers
    Jul. 2003, GENES & DEVELOPMENT, 17(13) (13), 1630 - 1645, English
    [Refereed]
    Scientific journal

  • Errol C. Friedberg, Fumio Hanaoka, Kiyoji Tanaka, Samuel H. Wilson, Akira Yasui, Kaoru Sugasawa, Tsukasa Matsunaga, Kiran Madura, Kevin Sweder, Bennett Van Houten, Priscilla Cooper, Tadahiro Shiomi, Arthur Grollman, Yusaku Nakabeppu, Susan Wallace, Masashi Takao, Yoshimichi Nakatsu, Teruhisa Tsuzuki, Shinya Oda, Shinichi Fukushige, Roger Woodgate, Zhigang Wang, Chikahide Masutani, Haruo Ohmori, Eiji Ohashi, Thomas Kunkel, Myron F. Goodman, Takehiko Nohmi, Eiichiro Sonoda, Masaru Yamaizumi, Mutsuo Sekiguchi, Graham Walker, Hisaji Maki, Kazuo Yamamoto, Kaoru Yoshiyama, Isao Kuraoka, Kenshi Komatsu, Alan Tomkinson, Hideo Shinagawa, John Tainer, Helfrid Hochegger, Takemi Enomoto, Roger Schultz, Akira Shimamoto, Vilhelm Bohr
    Elsevier, May 2003, DNA Repair, 2(5) (5), 639 - 652, English
    [Refereed]
    International conference proceedings

  • DNA bending by the human damage recognition complex XPC-HR23B
    A Janicijevic, K Sugasawa, Y Shimizu, F Hanaoka, N Wijgers, M Djurica, JHJ Hoeijmakers, C Wyman
    Mar. 2003, DNA REPAIR, 2(3) (3), 325 - 336, English
    [Refereed]
    Scientific journal

  • Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase.
    Yuichiro Shimizu, Shigenori Iwai, Fumio Hanaoka, Kaoru Sugasawa
    The XPC-HR23B complex recognizes various helix-distorting lesions in DNA and initiates global genome nucleotide excision repair. Here we describe a novel functional interaction between XPC-HR23B and thymine DNA glycosylase (TDG), which initiates base excision repair (BER) of G/T mismatches generated by spontaneous deamination of 5-methylcytosine. XPC-HR23B stimulated TDG activity by promoting the release of TDG from abasic sites that result from the excision of mismatched T bases. In the presence of AP endonuclease (APE), XPC-HR23B had an additive effect on the enzymatic turnover of TDG without significantly inhibiting the subsequent action of APE. Our observations suggest that XPC-HR23B may participate in BER of G/T mismatches, thereby contributing to the suppression of spontaneous mutations that may be one of the contributory factors for the promotion of carcinogenesis in xeroderma pigmentosum genetic complementation group C patients.
    Jan. 2003, The EMBO journal, 22(1) (1), 164 - 73, English, International magazine
    [Refereed]

  • The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH.
    Akio Uchida, Kaoru Sugasawa, Chikahide Masutani, Naoshi Dohmae, Marito Araki, Masayuki Yokoi, Yoshiaki Ohkuma, Fumio Hanaoka
    The xeroderma pigmentosum group C (XPC) protein specifically involved in genome-wide damage recognition for nucleotide excision repair (NER) was purified as a tight complex with HR23B, one of the two mammalian homologs of RAD23 in budding yeast. This XPC-HR23B complex exhibits strong binding affinity for single-stranded DNA, as well as preferential binding to various types of damaged DNA. To examine the structure-function relationship of XPC, a series of truncated mutant proteins were generated and assayed for various binding activities. The two domains participating in binding to HR23B and damaged DNA, respectively, were mapped within the carboxy-terminal half of XPC, which also contains an evolutionary conserved amino acid sequence homologous to the yeast RAD4 protein. We established that the carboxy-terminal 125 amino acids are dispensable for both HR23B and damaged DNA binding, while interactions with transcription factor IIH (TFIIH) are significantly impaired by truncation of this domain. Furthermore, deletion of the extreme carboxy-terminal domain totally abolished XPC activity in the cell-free NER reaction. These results suggest that following initial damage recognition, the carboxy terminus of XPC may be essential for the recruitment of TFIIH, and that most truncation mutations identified in XP-C patients result in non-functional proteins.
    Jun. 2002, DNA repair, 1(6) (6), 449 - 61, English, International magazine
    [Refereed]
    Scientific journal

  • Developmental defects and male sterility in mice lacking the ubiquitin-like DNA repair gene mHR23B.
    Jessica M Y Ng, Harry Vrieling, Kaoru Sugasawa, Marja P Ooms, J Anton Grootegoed, Jan T M Vreeburg, Pim Visser, Rudolph B Beems, Theo G M F Gorgels, Fumio Hanaoka, Jan H J Hoeijmakers, Gijsbertus T J van der Horst
    mHR23B encodes one of the two mammalian homologs of Saccharomyces cerevisiae RAD23, a ubiquitin-like fusion protein involved in nucleotide excision repair (NER). Part of mHR23B is complexed with the XPC protein, and this heterodimer functions as the main damage detector and initiator of global genome NER. While XPC defects exist in humans and mice, mutations for mHR23A and mHR23B are not known. Here, we present a mouse model for mHR23B. Unlike XPC-deficient cells, mHR23B(-/-) mouse embryonic fibroblasts are not UV sensitive and retain the repair characteristics of wild-type cells. In agreement with the results of in vitro repair studies, this indicates that mHR23A can functionally replace mHR23B in NER. Unexpectedly, mHR23B(-/-) mice show impaired embryonic development and a high rate (90%) of intrauterine or neonatal death. Surviving animals display a variety of abnormalities, including retarded growth, facial dysmorphology, and male sterility. Such abnormalities are not observed in XPC and other NER-deficient mouse mutants and point to a separate function of mHR23B in development. This function may involve regulation of protein stability via the ubiquitin/proteasome pathway and is not or only in part compensated for by mHR23A.
    Feb. 2002, Molecular and cellular biology, 22(4) (4), 1233 - 45, English, International magazine
    [Refereed]

  • A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex.
    Kaoru Sugasawa, Yuichiro Shimizu, Shigenori Iwai, Fumio Hanaoka
    The XPC-HR23B complex is involved in DNA damage recognition and the initiation of global genomic nucleotide excision repair (GG-NER). Our previous studies demonstrate that XPC-HR23B recognizes and binds DNA containing a helix distortion, regardless of the presence or absence of damaged bases. Here, we describe an extended analysis of the DNA binding specificity of XPC-HR23B using various defined DNA substrates. Although XPC-HR23B showed significantly higher affinity for single-stranded DNA than double-stranded DNA, specific secondary structures of DNA, involving a single- and double-strand junction, were strongly preferred by the complex. This indicates that the presence of bases, which cannot form normal Watson-Crick base pairs in double-stranded DNA, is a critical factor in determining the specificity of XPC-HR23B binding. A DNase I footprint analysis, using a looped DNA substrate, revealed that a single XPC-HR23B complex protected a distorted site in an asymmetrical manner, consistent with the preferred secondary structure. The specific binding of XPC-HR23B is undoubtedly an important molecular process, based on which NER machinery detects a wide variety of lesions that vary in terms of chemical structure during DNA repair.
    Jan. 2002, DNA repair, 1(1) (1), 95 - 107, English, International magazine
    [Refereed]

  • Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    M Araki, C Masutani, M Takemura, A Uchida, K Sugasawa, J Kondoh, Y Ohkuma, F Hanaoka
    Jun. 2001, JOURNAL OF BIOLOGICAL CHEMISTRY, 276(22) (22), 18665 - 18672, English
    [Refereed]
    Scientific journal

  • Diversity of the damage recognition step in the global genomic nucleotide excision repair in vitro
    R Kusumoto, C Masutani, K Sugasawa, S Iwai, M Araki, A Uchida, T Mizukoshi, F Hanaoka
    Apr. 2001, MUTATION RESEARCH-DNA REPAIR, 485(3) (3), 219 - 227, English
    [Refereed]
    Scientific journal

  • A multistep damage recognition mechanism for global genomic nucleotide excision repair
    K Sugasawa, T Okamoto, Y Shimizu, C Masutani, S Iwai, F Hanaoka
    Mar. 2001, GENES & DEVELOPMENT, 15(5) (5), 507 - 521, English
    [Refereed]
    Scientific journal

  • Novel functional interactions between nucleotide excision DNA repair proteins influencing the enzymatic activities of TFIIH, XPG, and ERCC1-XPF
    GS Winkler, K Sugasawa, APM Eker, WL de Laat, JHJ Hoeijmakers
    Jan. 2001, BIOCHEMISTRY, 40(1) (1), 160 - 165, English
    [Refereed]
    Scientific journal

  • Retinoblastoma susceptibility protein, Rb, possesses multiple BRCT-Ws, BRCA1 carboxyl-terminus-related W regions with DNA break-binding activity
    K Yamane, E Katayama, K Sugasawa, T Tsuruo
    Apr. 2000, ONCOGENE, 19(16) (16), 1982 - 1991, English
    [Refereed]
    Scientific journal

  • Araki M, Masutani C, Maekawa T, Watanabe Y, Yamada A, Kusumoto R, Sakai D, Sugasawa K, Ohkuma Y, Hanaoka F
    Mar. 2000, Mutation research, 459(2) (2), 147 - 160
    [Refereed]

  • The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA
    M Yokoi, C Masutani, T Maekawa, K Sugasawa, Y Ohkuma, F Hanaoka
    Mar. 2000, JOURNAL OF BIOLOGICAL CHEMISTRY, 275(13) (13), 9870 - 9875, English
    [Refereed]
    Scientific journal

  • Reconstitution of damage DNA excision reaction from SV40 minichromosomes with purified nucleotide excision repair proteins
    M Araki, C Masutani, T Maekawa, Y Watanabe, A Yamada, R Kusumoto, D Sakai, K Sugasawa, Y Ohkuma, F Hanaoka
    Mar. 2000, MUTATION RESEARCH-DNA REPAIR, 459(2) (2), 147 - 160, English
    [Refereed]
    Scientific journal

  • Interaction of hHR23 with S5a - The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
    H Hiyama, M Yokoi, C Masutani, K Sugasawa, T Maekawa, K Tanaka, JHJ Hoeijmakers, F Hanaoka
    Sep. 1999, JOURNAL OF BIOLOGICAL CHEMISTRY, 274(39) (39), 28019 - 28025, English
    [Refereed]
    Scientific journal

  • XPC蛋白質のNER初期反応に果たす役割についての解析
    荒木 真理人, 益谷 央豪, 楠本 理加, 渡辺 祥規, 前川 隆文, 大熊 芳明, 花岡 文雄, 菅澤 薫, 岩井 成憲
    (公社)日本薬学会, Mar. 1999, 日本薬学会年会要旨集, 119年会(3) (3), 114 - 114, Japanese

  • DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair
    WL de Laat, E Appeldoorn, K Sugasawa, E Weterings, NGJ Jaspers, JHJ Hoeijmakers
    Aug. 1998, GENES & DEVELOPMENT, 12(16) (16), 2598 - 2609, English
    [Refereed]
    Scientific journal

  • Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair
    K Sugasawa, JMY Ng, C Masutani, S Iwai, PJ van der Spek, APM Eker, F Hanaoka, D Bootsma, JHJ Hoeijmakers
    Aug. 1998, MOLECULAR CELL, 2(2) (2), 223 - 232, English
    [Refereed]
    Scientific journal

  • Identification and characterization of XPC-binding domain of hHR23B
    C Masutani, M Araki, K Sugasawa, PJ vanderSpek, A Yamada, A Uchida, T Maekawa, D Bootsma, JHJ Hoeijmakers, F Hanaoka
    Dec. 1997, MOLECULAR AND CELLULAR BIOLOGY, 17(12) (12), 6915 - 6923, English
    [Refereed]
    Scientific journal

  • Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity
    K Sugasawa, JMY Ng, C Masutani, T Maekawa, A Uchida, PJ vanderSpek, APM Eker, S Rademakers, C Visser, A Aboussekhra, RD Wood, F Hanaoka, D Bootsma, JHJ Hoeijmakers
    Dec. 1997, MOLECULAR AND CELLULAR BIOLOGY, 17(12) (12), 6924 - 6931, English
    [Refereed]
    Scientific journal

  • Mammalian nucleotide excision repair and syndromes
    W Vermeulen, J deBoer, E Citterio, AJ vanGool, GTJ vanderHorst, NGJ Jaspers, WL deLaat, AM Sijbers, PJ vanderSpek, K Sugasawa, G Weeda, GS Winkler, D Bootsma, JM Egly, JHJ Hoeijmakers
    Feb. 1997, BIOCHEMICAL SOCIETY TRANSACTIONS, 25(1) (1), 309 - 315, English
    [Refereed]
    Scientific journal

  • HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro
    K Sugasawa, C Masutani, A Uchida, T Maekawa, PJ vanderSpek, D Bootsma, JHJ Hoeijmakers, F Hanaoka
    Sep. 1996, MOLECULAR AND CELLULAR BIOLOGY, 16(9) (9), 4852 - 4861, English
    [Refereed]
    Scientific journal

  • XPC and human homologs of RAD23: Intracellular localization and relationship to other nucleotide excision repair complexes
    PJ vanderSpek, A Eker, S Rademakers, C Visser, K Sugasawa, C Masutani, F Hanaoka, D Bootsma, JHJ Hoeijmakers
    Jul. 1996, NUCLEIC ACIDS RESEARCH, 24(13) (13), 2551 - 2559, English
    [Refereed]
    Scientific journal

  • T SHIMAMOTO, T TANIMURA, Y YONEDA, Y KOBAYAKAWA, K SUGASAWA, F HANAOKA, M OKA, Y OKADA, K TANAKA, K KOHNO
    Sep. 1995, JOURNAL OF BIOLOGICAL CHEMISTRY, 270(38) (38), 22452 - 22459, English
    [Refereed]
    Scientific journal

  • DNA-REPAIR PROTEIN XPA BINDS REPLICATION PROTEIN-A (RPA)
    T MATSUDA, M SAIJO, KURAOKA, I, T KOBAYASHI, Y NAKATSU, A NAGAI, T ENJOJI, C MASUTANI, K SUGASAWA, F HANAOKA, A YASUI, K TANAKA
    Feb. 1995, JOURNAL OF BIOLOGICAL CHEMISTRY, 270(8) (8), 4152 - 4157, English
    [Refereed]
    Scientific journal

  • CHROMOSOMAL LOCALIZATION OF 3 REPAIR GENES - THE XERODERMA-PIGMENTOSUM GROUP-C GENE AND 2 HUMAN HOMOLOGS OF YEAST RAD23
    PJ VANDERSPEK, EME SMIT, HB BEVERLOO, K SUGASAWA, C MASUTANI, F HANAOKA, JHJ HOEIJMAKERS, A HAGEMEIJER
    Oct. 1994, GENOMICS, 23(3) (3), 651 - 658, English
    [Refereed]
    Scientific journal

  • PURIFICATION AND CLONING OF A NUCLEOTIDE EXCISION-REPAIR COMPLEX INVOLVING THE XERODERMA-PIGMENTOSUM GROUP-C PROTEIN AND A HUMAN HOMOLOG OF YEAST RAD23
    C MASUTANI, K SUGASAWA, J YANAGISAWA, T SONOYAMA, M UI, T ENOMOTO, K TAKIO, K TANAKA, PJ VANDERSPEK, D BOOTSMA, JHJ HOEIJMAKERS, F HANAOKA
    Apr. 1994, EMBO JOURNAL, 13(8) (8), 1831 - 1843, English
    [Refereed]
    Scientific journal

  • CELL-FREE REPAIR OF UV-DAMAGED SIMIAN VIRUS-40 CHROMOSOMES IN HUMAN CELL-EXTRACTS .1. DEVELOPMENT OF A CELL-FREE SYSTEM DETECTING EXCISION REPAIR OF UV-IRRADIATED SV40 CHROMOSOMES
    K SUGASAWA, C MASUTANI, F HANAOKA
    Apr. 1993, JOURNAL OF BIOLOGICAL CHEMISTRY, 268(12) (12), 9098 - 9104, English
    [Refereed]
    Scientific journal

  • CELL-FREE REPAIR OF UV-DAMAGED SIMIAN VIRUS-40 CHROMOSOMES IN HUMAN CELL-EXTRACTS .2. DEFECTIVE-DNA REPAIR SYNTHESIS BY XERODERMA-PIGMENTOSUM CELL-EXTRACTS
    C MASUTANI, K SUGASAWA, H ASAHINA, K TANAKA, F HANAOKA
    Apr. 1993, JOURNAL OF BIOLOGICAL CHEMISTRY, 268(12) (12), 9105 - 9109, English
    [Refereed]
    Scientific journal

  • ABROGATION OF P53-MEDIATED TRANSACTIVATION BY SV40 LARGE T-ANTIGEN
    K SEGAWA, A MINOWA, K SUGASAWA, T TAKANO, F HANAOKA
    Mar. 1993, ONCOGENE, 8(3) (3), 543 - 548, English
    [Refereed]
    Scientific journal

  • COMPLEMENTATION BY A CLONED HUMAN UBIQUITIN-ACTIVATING ENZYME E1 OF THE S-PHASE-ARRESTED MOUSE FM3A CELL MUTANT WITH THERMOLABILE E1
    D AYUSAWA, S KANEDA, Y ITOH, H YASUDA, Y MURAKAMI, K SUGASAWA, F HANAOKA, T SENO
    Apr. 1992, CELL STRUCTURE AND FUNCTION, 17(2) (2), 113 - 122, English
    [Refereed]
    Scientific journal

  • NONCONSERVATIVE SEGREGATION OF PARENTAL NUCLEOSOMES DURING SIMIAN VIRUS-40 CHROMOSOME-REPLICATION INVITRO
    K SUGASAWA, Y ISHIMI, T EKI, J HURWITZ, A KIKUCHI, F HANAOKA
    Feb. 1992, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 89(3) (3), 1055 - 1059, English
    [Refereed]
    Scientific journal

  • TOPOISOMERASE-II PLAYS AN ESSENTIAL ROLE AS A SWIVELASE IN THE LATE STAGE OF SV40 CHROMOSOME-REPLICATION INVITRO
    Y ISHIMI, K SUGASAWA, F HANAOKA, T EKI, J HURWITZ
    Jan. 1992, JOURNAL OF BIOLOGICAL CHEMISTRY, 267(1) (1), 462 - 466, English
    [Refereed]
    Scientific journal

  • REPLICATION OF THE SIMIAN VIRUS-40 CHROMOSOME WITH PURIFIED PROTEINS
    Y ISHIMI, K SUGASAWA, F HANAOKA, A KIKUCHI
    Aug. 1991, JOURNAL OF BIOLOGICAL CHEMISTRY, 266(24) (24), 16141 - 16148, English
    [Refereed]
    Scientific journal

  • ASSEMBLY OF NASCENT DNA INTO NUCLEOSOME STRUCTURES IN SIMIAN-VIRUS 40 CHROMOSOMES BY HELA-CELL EXTRACT
    K SUGASAWA, Y MURAKAMI, N MIYAMOTO, F HANAOKA, M UI
    Oct. 1990, JOURNAL OF VIROLOGY, 64(10) (10), 4820 - 4829, English
    [Refereed]
    Scientific journal

  • HETEROGENEOUS ASSEMBLY OF NASCENT CORE HISTONES TO FORM NUCLEOSOMAL HISTONE OCTAMERS IN MOUSE FM3A CELLS
    K SUGASAWA, Y ISHIMI, M YAMADA, F HANAOKA, M UI
    Oct. 1989, EUROPEAN JOURNAL OF BIOCHEMISTRY, 185(1) (1), 55 - 61, English
    [Refereed]
    Scientific journal

  • CHARACTERIZATION OF THE 100,000 DALTON MATERIAL PRODUCED BY CHROMATIN CROSS-LINKING REACTION WITH DITHIO-BIS(SUCCINIMIDYL PROPIONATE)
    K SUGASAWA, Y ISHIMI, F HANAOKA, M YAMADA
    Dec. 1986, JOURNAL OF BIOCHEMISTRY, 100(6) (6), 1543 - 1550, English
    [Refereed]
    Scientific journal

  • RAPID PURIFICATION OF NUCLEOSOME ASSEMBLY PROTEIN (AP-I) AND PRODUCTION OF MONOCLONAL-ANTIBODIES AGAINST IT
    Y ISHIMI, W SATO, M KOJIMA, K SUGASAWA, F HANAOKA, MA YAMADA
    Dec. 1985, CELL STRUCTURE AND FUNCTION, 10(4) (4), 373 - 382, English
    [Refereed]
    Scientific journal

  • PURIFICATION AND INITIAL CHARACTERIZATION OF A PROTEIN WHICH FACILITATES ASSEMBLY OF NUCLEOSOME-LIKE STRUCTURE FROM MAMMALIAN-CELLS
    Y ISHIMI, J HIROSUMI, W SATO, K SUGASAWA, S YOKOTA, F HANAOKA, MA YAMADA
    1984, EUROPEAN JOURNAL OF BIOCHEMISTRY, 142(3) (3), 431 - 439, English
    [Refereed]
    Scientific journal

■ MISC
  • Investigating the TDP1-mediated error-prone repair of a ribonucleotide embedded into the genome
    黛結衣子, 高藤賢, 中谷一真, 菅澤薫, 浦聖恵, 佐々彰
    2021, 日本環境変異原ゲノム学会大会プログラム・要旨集, 50th

  • Molecular mechanism of excessive immune response caused by aberrant DNA repair
    高藤賢, 立川明日香, 黛結衣子, 中谷一真, 菅澤薫, 浦聖恵, 佐々彰
    2021, 日本環境変異原ゲノム学会大会プログラム・要旨集, 50th

  • Tyrosyl-DNA phosphodiesterasesはDNA中のリボヌクレオチドを起因とする突然変異形成に関与する
    竹石歩奈, 古樫浩之, 小田切瑞基, 笹沼博之, 武田俊一, 安井学, 本間正充, 菅澤薫, 浦聖恵, 佐々彰
    2020, 日本分子生物学会年会プログラム・要旨集(Web), 43rd

  • Molecular mechanism of DNA damage recognition for global genomic nucleotide excision repair: A defense system against UV-induced skin cancer
    SUGASAWA KAORU
    Springer (eds. Nishigori Chikako and Kaoru Sugasawa), Jan. 2019, DNA Repair Disorders, 1 - 23, English
    [Refereed]
    Introduction scientific journal

  • Chikako Nishigori, Kaoru Sugasawa
    Springer Singapore, 01 Jan. 2018, DNA Repair Disorders, 1 - 221, English
    Others

  • リボヌクレオチドが誘発する奇異突然変異とその防御機構
    佐々彰, 安井学, 竹石歩奈, 原田佳歩, 鈴木慈, 津田雅貴, 笹沼博之, 武田俊一, 菅澤薫, 本間正充, 浦聖恵
    2018, 日本遺伝学会大会プログラム・予稿集, 90th

  • DNA中のリボヌクレオチドが引き起こす特異な突然変異とその誘発機構の解析
    竹石歩奈, 安井学, 笹沼博之, 武田俊一, 菅澤薫, 本間正充, 浦聖恵, 佐々彰
    2018, 日本環境変異原学会大会プログラム・要旨集, 47th

  • Truncated XPA protein could not interact with TFIIH but presented mild clinical manifestations
    E. Nakano, M. Tusjimoto, S. Takeuchi, R. Ono, T. Masaki, K. Sugasawa, C. Nishigori
    May 2017, JOURNAL OF INVESTIGATIVE DERMATOLOGY, 137(5) (5), S131 - S131, English
    Summary international conference

  • DNA中のリボヌクレオチドが引き起こす突然変異とその抑制機構
    佐々彰, 安井学, 笹沼博之, 武田俊一, 菅澤薫, 本間正充, 浦聖恵
    2017, 日本生化学会大会(Web), 90th

  • リボヌクレオチドが誘発する突然変異の抑制におけるDNA修復機構の役割
    佐々彰, 安井学, 笹沼博之, 武田俊一, 菅澤薫, 本間正充, 浦聖恵
    2017, 日本環境変異原学会大会プログラム・要旨集, 46th

  • 紫外線によるDNAの損傷とがん化のメカニズム (特集 紫外線が原因で起こる皮膚トラブルと化粧品開発)
    横井 雅幸, 菅澤 薫
    技術情報協会, Oct. 2016, Cosmetic stage, 11(1) (1), 9 - 15, Japanese

  • Kaoru Sugasawa
    Elsevier B.V., 01 Aug. 2016, DNA Repair, 44, 110 - 117, English
    [Refereed]
    Book review

  • Tripartite DNA Lesion Recognition and Verification by XPC, TFIIH, and XPA in Nucleotide Excision Repair
    Filip M. Golebiowski, Chia-Lung Li, Yuki Onishi, Nadine L. Samara, Kaoru Sugasawa, Wei Yang
    Apr. 2016, FASEB JOURNAL, 30, English
    Summary international conference

  • Tripartite DNA Lesion Recognition and Verification by XPC, TFIIH, and XPA in Nucleotide Excision Repair
    Filip M. Golebiowski, Chia-Lung Li, Yuki Onishi, Nadine L. Samara, Kaoru Sugasawa, Wei Yang
    Apr. 2016, FASEB JOURNAL, 30, English
    Summary international conference

  • Fumio Hanaoka, Kaoru Sugasawa
    Springer Japan, 01 Jan. 2016, DNA Replication, Recombination, and Repair: Molecular Mechanisms and Pathology, 1 - 555, English
    Others

  • Fumio Hanaoka, Kaoru Sugasawa
    Springer Japan, 01 Jan. 2016, DNA Replication, Recombination, and Repair: Molecular Mechanisms and Pathology, v - vi, English
    Others

  • Wataru Sakai, Kaoru Sugasawa
    Springer Japan, 01 Jan. 2016, DNA Replication, Recombination, and Repair: Molecular Mechanisms and Pathology, 155 - 174, English
    [Refereed][Invited]
    Introduction other

  • Studies on the de-ubiquitination mechanism for the xeroderma pigmentosum group C protein in UV damage response
    Wataru Sakai, Aiko Kishimoto, Takeshi Matsui, Jun-ichi Akagi, Kaoru Sugasawa
    Dec. 2015, GENES & GENETIC SYSTEMS, 90(6) (6), 397 - 397, English
    Summary international conference

  • 酸化的DNA/RNA脱メチル化酵素ALKBH3の機能解析
    稲瀬 安希, 太田 奈緒, 本橋 ほづみ, 菅澤 薫
    (公社)日本生化学会, Dec. 2015, 日本生化学会大会・日本分子生物学会年会合同大会講演要旨集, 88回・38回, [3P1218] - [3P1218], English

  • 酸化的DNA/RNA脱メチル化酵素ALKBH3の発現変化は細胞増殖や代謝に影響を与える
    稲瀬 安希, 本橋 ほづみ, 菅澤 薫
    日本癌学会, Oct. 2015, 日本癌学会総会記事, 74回, P - 3148, English

  • Post-translational modifications coordinating recognition and repair of UV-induced DNA damage
    Syota Matsumoto, Masaki Akita, Wataru Sakai, Kaoru Sugasawa
    Apr. 2015, DNA REPAIR, 28, 144 - 144, English
    Summary international conference

  • ヌクレオチド除去修復を制御するタンパク質リン酸化の解析
    木下実, 木下実, 戸根大輔, 戸根大輔, 岩井成憲, 菅澤薫, 菅澤薫
    2015, 日本生化学会大会(Web), 88th

  • 塩基除去修復因子チミンDNAグリコシラーゼの構造活性相関と機能制御
    中村知史, 中村知史, 村上浩一, 村上浩一, 松田俊, 松田知成, 上原芳彦, 小野哲也, 西谷秀男, 菅澤薫, 菅澤薫
    2015, 日本生化学会大会(Web), 88th

  • Studies on the de-ubiquitylation mechanism of the xeroderma pigmentosum group C protein
    Aiko Kishimoto, Junichi Akagi, Takeshi Matsui, Wataru Sakai, Kaoru Sugasawa
    Dec. 2014, GENES & GENETIC SYSTEMS, 89(6) (6), 312 - 312, English
    Summary international conference

  • GENOTYPE -PHENOTYPE CORRELATION AMONG XERODERMA PIGMENTOSUM COMPLEMENTATION GROUP D
    Eiji Nakano, Ryusuke Ono, Taro Masaki, Seiji Takeuchi, Yutaka Takaoka, Kaoru Sugasawa, Chikako Nishigori
    Oct. 2014, JOURNAL OF DERMATOLOGY, 41, 14 - 14, English
    Summary international conference

  • 紫外線損傷修復におけるXPCタンパク質の脱ユビキチン化機構の解析
    岸本藍子, 赤木純一, 松井豪志, 酒井恒, 菅澤薫
    31 Aug. 2014, 日本遺伝学会大会プログラム・予稿集, 86th, 99, Japanese

  • ヌクレオチド除去修復におけるDNA損傷認識機構の解析
    大西優貴, 大西優貴, 戸根大輔, 戸根大輔, 木下実, 木下実, 岩井成憲, 菅澤薫, 菅澤薫
    2014, 日本分子生物学会年会プログラム・要旨集(Web), 37th

  • A novel function of FANCD2 protein in apoptosis signaling
    Wataru Sakai, Kaoru Sugasawa
    Dec. 2013, GENES & GENETIC SYSTEMS, 88(6) (6), 361 - 361, English
    Summary international conference

  • 紫外線損傷DNAを含むヌクレオソームの生化学的および構造生物学的解析
    越阪部 晃永, 堀越 直樹, 立和名 博昭, 香川 亘, 安田 武嗣, 花岡 文雄, 菅澤 薫, 岩井 成憲, 胡桃坂 仁志
    (公社)日本生化学会, Sep. 2013, 日本生化学会大会プログラム・講演要旨集, 86回, 2T14a - 07, Japanese

  • Studies on the de-ubiquitylation mechanism of the xeroderma pigmentosum group C protein
    Junichi Akagi, Takeshi Matsui, Wataru Sakai, Kaoru Sugasawa
    Dec. 2012, GENES & GENETIC SYSTEMS, 87(6) (6), 386 - 386, English
    Summary international conference

  • Alex Pines, Mischa G. Vrouwe, Jurgen A. Marteijn, Dimitris Typas, Martijn S. Luijsterburg, Medine Cansoy, Paul Hensbergen, Andre Deelder, Anton de Groot, Syota Matsumoto, Kaoru Sugasawa, Nicolas Thoma, Wim Vermeulen, Harry Vrieling, Leon Mullenders
    Oct. 2012, JOURNAL OF CELL BIOLOGY, 199(2) (2), 235 - 249, English
    [Refereed]
    Introduction scientific journal

  • 紫外線によるDNA損傷の修復を促進するDDB2の構造と機能制御
    松本 翔太, 安田 武嗣, Fischer Eric, Thoma Nicolas, 花岡 文雄, 菅澤 薫
    (一社)日本放射線影響学会, Sep. 2012, 日本放射線影響学会大会講演要旨集, 55回, 126 - 126, Japanese

  • DNA損傷応答に関わる新規アセチル化標的タンパク質の同定
    安田武嗣, 齋藤健吾, 香川亘, 荻朋男, 鈴木健祐, 堂前直, 日野拓也, 中沢由華, 中邑愛, 羽澤勝治, 花岡文雄, 菅澤薫, 岡安隆一, 胡桃坂仁志, 田嶋克史
    31 Aug. 2012, 日本遺伝学会大会プログラム・予稿集, 84th, 100, Japanese

  • 紫外線損傷修復におけるXPCタンパク質の脱ユビキチン化機構の解析
    赤木純一, 松井豪志, 酒井恒, 菅澤薫
    31 Aug. 2012, 日本遺伝学会大会プログラム・予稿集, 84th, 72, Japanese

  • Molecular Basis of DNA Damage Recognition in Nucleotide Excision Repair
    菅澤 薫
    放射線生物研究会, Jun. 2012, 放射線生物研究, 47(2) (2), 95 - 111, Japanese

  • 無細胞再構成系によるヌクレオチド除去修復活性制御因子の探索
    戸根大輔, 戸根大輔, 吉野健一, 岩井成憲, 菅澤薫, 菅澤薫
    2012, 日本分子生物学会年会プログラム・要旨集(Web), 35th

  • ゲノム安定維持に関わるcentrin-2の新たな機能
    菅澤薫, 菅澤薫, 西良太郎, 酒井恒, 戸根大輔, 戸根大輔, 花岡文雄
    2012, 日本分子生物学会年会プログラム・要旨集(Web), 35th

  • DNA損傷によるヒトRad52タンパク質のアセチル化は,DNA二重鎖切断部位への集積に必要である
    安田武嗣, 齋藤健吾, 香川亘, 荻朋男, 鈴木健祐, 堂前直, 日野拓也, 中沢由華, 早乙女(中邑)愛, 加藤宝光, GENET Matthew, 羽澤勝治, 冨田雅典, 花岡文雄, 菅澤薫, JEGGO Penny, 岡安隆一, 田嶋克史, 胡桃坂仁志
    2012, 日本分子生物学会年会プログラム・要旨集(Web), 35th, 2W5II-1 (WEB ONLY), Japanese

  • ヒト間葉系幹細胞におけるヒトRad52タンパク質のDNA損傷によるアセチル化誘導
    早乙女, 中邑, 愛, 安田武嗣, 齋藤健吾, 香川亘, 荻朋男, 鈴木健祐, 堂前直, 日野拓也, 中沢由華, 羽澤勝治, 花岡文雄, 菅澤薫, 岡安隆一, 胡桃坂仁志, 田嶋克史
    2012, 日本分子生物学会年会プログラム・要旨集(Web), 35th, 1P-0201 (WEB ONLY), Japanese

  • Hanspeter Naegeli, Kaoru Sugasawa
    Jul. 2011, DNA REPAIR, 10(7) (7), 673 - 683, English
    Book review

  • DNA damage recognition for mammalian global genome nucleotide excision repair
    Sugasawa Kaoru
    2011, DNA repair, Vol. , No. , pp. 453-476, English
    [Refereed]
    Introduction scientific journal

  • K. Sugasawa
    Jan. 2011, BIOCHEMISTRY-MOSCOW, 76(1) (1), 16 - 23, English
    [Refereed]
    Book review

  • DNA損傷認識蛋白質DDB2のN末端領域の機能解析(Functional analysis of the N-terminal domain of the DNA damage recognition protein DDB2)
    松本 翔太, 安田 武嗣, 堂前 直, 村上 浩一, 西 良太郎, 花岡 文雄, 菅澤 薫
    (公社)日本生化学会, Dec. 2010, 日本生化学会大会・日本分子生物学会年会合同大会講演要旨集, 83回・33回, 1T12 - 9, English

  • Genotoxic stress targets Fanconi anemia group D2 protein for fragmentation by the caspase-mediated pathway
    Wataru Sakai, Kaoru Sugasawa
    Feb. 2010, GENES & GENETIC SYSTEMS, 85(1) (1), 86 - 86, English
    Summary international conference

  • Kaoru Sugasawa
    Aug. 2009, DNA REPAIR, 8(8) (8), 969 - 972, English
    [Refereed]
    Introduction scientific journal

  • Regulation of damage recognition in mammalian global genomic nucleotide excision repair.
    Sugasawa Kaoru
    Aug. 2009, Mutat Res., 685(1-2):29-37, 29 - 37
    [Refereed]
    Introduction scientific journal

  • Kaoru Sugasawa
    May 2009, MOLECULAR CELL, 34(4) (4), 403 - 404, English
    [Refereed]
    Others

  • 色素性乾皮症遺伝子産物によるDNA損傷認識機構
    SUGASAWA Kaoru
    医歯薬出版, Jan. 2009, 医学のあゆみ, 228: 137-142(2) (2), 137 - 142, Japanese
    [Refereed]
    Introduction scientific journal

  • Fumio Yatagai, Kaoru Sugasawa, Shuichi Enomoto, Masamitsu Honma
    2009, Journal of Radiation Research, 50(5) (5), 407 - 413, English
    [Refereed]
    Book review

  • Kaoru Sugasawa
    Mar. 2008, CARCINOGENESIS, 29(3) (3), 455 - 465, English
    Book review
    Link to Kobe Univ. Repository (Kernel)

  • Kaoru Sugasawa, Fumio Hanaoka
    Oct. 2007, NATURE STRUCTURAL & MOLECULAR BIOLOGY, 14(10) (10), 887 - 888, English
    Others

  • Sensing of DNA damage by XPC/Rad4: one protein for many lesions.
    Kaoru Sugasawa, Fumio Hanaoka
    Oct. 2007, Nature structural & molecular biology, 14(10) (10), 887 - 8, English, International magazine
    [Refereed]
    Introduction scientific journal

  • ヌクレオチド除去修復における損傷認識とユビキチン化
    菅澤薫, 志村勉, 赤木純一, 西良太郎
    2007, 生化学, 3W23-3, Japanese

  • Kaoru Sugasawa
    Sep. 2006, JOURNAL OF MOLECULAR HISTOLOGY, 37(5-7) (5-7), 189 - 202, English
    Book review

  • クロマチン構造を介したヌクレオチド除去修復
    安田 武嗣, 菅澤 薫, 塩見 忠博, 花岡 文雄
    放射線生物研究会, 20 Dec. 2005, 放射線生物研究, 40(4) (4), 345 - 359, Japanese

  • S2-2 Recognition and repair of DNA base lesions for protection against cancer(Symposium(2)"Challenge against carcinogenesis, a big Black Box")
    Sugasawa Kaoru
    日本環境変異原学会, 2005, 日本環境変異原学会大会プログラム・要旨集, (34) (34), 78 - 78, English

  • XPC複合体およびUV‐DDBの損傷DNA結合活性に対するヌクレオソーム構造の影響
    安田武嗣, 菅沢薫, 清水祐一郎, 西良太郎, 岩井成憲, 塩見忠博, 花岡文雄
    25 Nov. 2004, 日本分子生物学会年会プログラム・講演要旨集, 27th, 637, Japanese

  • Functional analysis of centrin2 in XPC protein complex
    Kaoru Sugasawa, Ryotaro Nishi, Yuki Okuda, Toshio Mori, Fumio Hanaoka
    May 2004, CELL STRUCTURE AND FUNCTION, 29, 63 - 63, English
    Summary international conference

  • Ubiquitylation of XPC protein by DDB-E3 complex
    K. Sugasawa, Y. Okuda, M. Saijo, R. Nishi, Y. Shimizu, N. Matsuda, K. Tanaka, K. Tanaka, O. F. Hanaoka
    May 2004, CELL STRUCTURE AND FUNCTION, 29, 11 - 11, English
    Summary international conference

  • ヌクレオソーム構造によるXPC蛋白質複合体の非特異的DNA結合の抑制はヌクレオチド除去修復の特異性を高める
    安田武嗣, 菅沢薫, 岩井成徳, 塩見忠博, 花岡文雄
    25 Nov. 2003, 日本分子生物学会年会プログラム・講演要旨集, 26th, 497, Japanese

  • XPC‐HR23Bの非特異的DNA結合はヌクレオソーム構造によって抑制される
    安田武嗣, 菅沢薫, 岩井成憲, 塩見忠博, 花岡文雄
    06 Oct. 2003, 日本放射線影響学会大会講演要旨集, 46th, 126, Japanese

  • HR23Bユビキチン相同ドメイン-プロテアソームS5aサブユニットユビキチン結合モチーフ複合体の構造解析
    藤原健一朗, 天野剛志, 菅沢薫, JEE J-G, 大木出, 児嶋長次郎, 栃尾豪人, 広明秀一, 花岡文雄
    2003, NMR討論会講演要旨集, 42nd

  • プロテアソームS5aサブユニットユビキチン結合モチーフとhHR23Bユビキチン相同ドメイン複合体の構造解析
    藤原健一朗, 天野剛志, 菅沢薫, JEE J G, 大木出, 児嶋長次郎, 栃尾豪人, 広明秀一, 花岡文雄
    2003, 日本分子生物学会年会プログラム・講演要旨集, 26th

  • 74 Nucleosome structure suppresses non-specific DNA binding of XPC-HR23B(Radiation sensitivities in cells & tissues, Abstracts of the 46th Annual Meeting of the Japan Radiation Research Society) :
    YASUDA Takeshi, SUGASAWA Kaoru, IWAI Shigenori, SHIOMI Tadahiro, HANAOKA Fumio
    the Japan Radiation Research Society, 2003, Journal of radiation research, 44(4) (4), 405 - 405, English

  • Thomas Hey, Georg Lipps, Kaoru Sugasawa, Shigenori Iwai, Fumio Hanaoka, Gerhard Krauss
    The XPC-HR23B complex is a prime candidate for the initial damage recognition step during global genome nucleotide excision repair. A specific interaction between the XPC-HR23B complex and various types of damaged DNA substrates has been demonstrated in recent work by electrophoretic mobility shift assays or immunoprecipitation. Although these studies allowed the estimation of relative binding affinities for the different types of lesions, the presence of large amounts of competitor DNA or the need for glutaraldehyde fixation prevented the quantification of equilibrium constants. We have performed a quantitative study on the binding of XPC to damaged DNA using fluorescence anisotropy measurements. The XPC-HR23B complex binds with high affinity (K(D) approximately 1-3 nM) to fluorescent 36 bp DNA fragments containing a single cisplatin 1,3-intrastrand adduct or a six-nucleotide mispaired region. From stoichiometric titration experiments, it is concluded that approximately 70% of the XPC-HR23B preparation is active in DNA binding. Binding experiments employing fluorescent probes with a single defined photoproduct reveal a 30-fold preference of XPC for 6,4-photoproducts as compared to a cyclobutane dimer. Competition experiments with undamaged and damaged plasmid DNA indicate that the XPC-HR23B complex discriminates between damaged and undamaged sites with high specificity. The specificity factor is between 100 and 3000, depending on the number of nonspecific sites considered in the calculations. Upon addition of XPA to the XPC binding reaction mixtures, it was not possible to detect cooperative ternary complex formation on the platinated 36 bp probe.
    28 May 2002, Biochemistry, 41(21) (21), 6583 - 7, English, International magazine
    [Refereed]

  • Functions of the DNA Damage Recognition Factor for Mammalian Nucleotide Excision Repair :
    SUGASAWA Kaoru, SHIMIZU Yuichiro, HANAOKA Fumio
    the Japan Radiation Research Society, 2002, Journal of radiation research, 43(4) (4), 416 - 416, English

  • C群色素性乾皮症(XPC)タンパク質の生細胞核内でのタンパク質間の相互作用と局在
    奥村 浩美, 児玉 由香, 石館 文善, 田仲 昭子, 菅澤 薫, 花岡 文雄
    31 Jul. 2001, Tissue culture research communications : the journal of experimental & applied cell culture research = 組織培養研究, 20(2) (2), 105 - 105, Japanese

  • Effects of Gravity Change on Protein : protein Interaction
    MASAKI Michiko, YAMAUCHI Yukika, OKUMURA Hiromi, SUGASAWA Kaoru, HANAOKA Fumio, TANAKA Akiko
    Oct. 2000, 宇宙生物科学 = Biological sciences in space, 14(3) (3), 264 - 265, Japanese

  • Cell Cycle Regulation after DNA Damage in Nucleotide Excision Repair Deficient Cells
    OKUMURA Hiromi, YAMAUCHI Yukika, TANAKA Akiko, SUGASAWA Kaoru, HANAOKA Fumio
    日本組織培養学会, 30 Jun. 2000, Tissue culture research communications : the journal of experimental & applied cell culture research = 組織培養研究, 19(2) (2), 68 - 68, Japanese

  • Damaged DNA binding activities of the XPC-hHR23B complex
    KUSUMOTO Rika, MASUTANI Chikahide, IWAI Shigenori, ARAKI Marito, SUGASAWA Kaoru, HANAOKA Fumio
    01 Dec. 1998, 日本分子生物学会年会プログラム・講演要旨集, 21, 371 - 371, Japanese

  • Function of the XPC protein complex in nucleotide excision repair
    SUGASAWA Kaoru, MASUTANI Chikahide, HOEIJMAKERS Jan H. J., HANAOKA Fumio
    01 Dec. 1998, 日本分子生物学会年会プログラム・講演要旨集, 21, 371 - 371, Japanese

  • Studies on XPC functional domains
    UCHIDA Akio, MAEKAWA Takafumi, MASUTANI Chikahide, YOKOI Masayuki, SUGASAWA Kaoru, OHKUMA Yoshiaki, HANAOKA Fumio
    01 Dec. 1998, 日本分子生物学会年会プログラム・講演要旨集, 21, 370 - 370, Japanese

  • Analysis of the interaction between hJR23A/B nad S5a
    HIYAMA Hideki, YOKOI Masayuki, MASUTANI Chikashide, SUGASAWA Kaoru, MAEKAWA Takafumi, TANAKA Keiji, HANAOKA Fumio
    01 Dec. 1998, 日本分子生物学会年会プログラム・講演要旨集, 21, 371 - 371, Japanese

  • 真核細胞ヌクレオチド除去修復の分子機構
    花岡 文雄, 益谷 央豪, 前川 隆文, 菅澤 薫, 大熊 芳明
    Aug. 1996, 日本分子生物学会年会プログラム・講演要旨集, 19, 75 - 75, Japanese

  • XPC-HHR23B複合体の機能の解析
    益谷 央豪, 荒木 真理人, 尾幡 裕子, 内田 章夫, 前川 隆文, 菅澤 薫, 花岡 文雄
    01 Aug. 1996, 日本分子生物学会年会プログラム・講演要旨集, 19, 778 - 778, Japanese

  • XPC/HHR23B蛋白質合体の相互作用
    尾幡 裕子, 前川 隆文, 益谷 央豪, 内田 章夫, 荒木 真理人, 菅澤 薫, 花岡 文雄
    01 Aug. 1996, 日本分子生物学会年会プログラム・講演要旨集, 19, 778 - 778, Japanese

  • M KUDO, K SUGASAWA, T HORI, T ENOMOTO, F HANAOKA, M UI
    Jan. 1991, EXPERIMENTAL CELL RESEARCH, 192(1) (1), 110 - 117, English

  • CORRELATION BETWEEN CELL-PROLIFERATION AND REGULARITY OF NUCLEOSOME STRUCTURE
    K SUGASAWA, Y ISHIMI, F HANAOKA, M UI
    Dec. 1987, CELL STRUCTURE AND FUNCTION, 12(6) (6), 649 - 649, English
    Summary international conference

■ Books And Other Publications
  • 紫外線によるDNAの損傷とがん化のメカニズム
    Yokoi,M, Sugasawa, K
    Joint work, 技術情報協会, Oct. 2016, Japanese
    General book

  • DNA Replication, Recombination and Repair: Molecular Mechanisms and Pathology
    Kaoru Sugasawa, Fumio Hanaoka
    Joint editor, Springer, 2016, English
    Scholarly book

  • 光老化科学の最前線
    酒井 恒, 菅澤 薫
    Joint work, シーエムシー出版, Apr. 2015, Japanese
    Scholarly book

  • DNA Repair (Kruman, I. ed.)
    SUGASAWA Kaoru
    Joint work, InTech, Oct. 2007, English
    Scholarly book

  • DNA Repair disorders
    錦織, 千佳子, 菅澤, 薫
    Springer, English, ISBN: 9789811067211

■ Lectures, oral presentations, etc.
  • DNA の構造的要因から探るヌクレオチド除去修復制御機構
    古園英嗣, 松山宏生, 多田遥人, 日下部将之, 松本翔太, 鯨井智也, 越後谷健太, 胡桃坂仁志, 菅澤薫
    第42回染色体ワークショップ・第23回核ダイナミクス研究会, Jan. 2025, Japanese
    Poster presentation

  • 脂肪族アルデヒドの代謝異常がゲノム安定性に及ぼす影響
    酒井恒, 䑺谷智也, 梶本武利, 岡田太郎, 篠原正和, 横井雅幸, 菅澤薫
    日本環境変異原ゲノム学会第53回大会, Dec. 2024, Japanese
    [Invited]
    Invited oral presentation

  • CRL4Cdt2のDNA合成部位への適切な集積と解離が細胞周期進行を制御する
    戸次龍哉, 日下部将之, 上野晃子, 塩見泰史, 菅澤薫, 林晃世, 西谷秀男
    第47回日本分子生物学会年会, Nov. 2024, Japanese
    Poster presentation

  • クライオ電子顕微鏡によるクロマチン上の紫外線損傷修復メカニズムの解明
    松本翔太, 滝沢由政, 小笠原光雄, 橋本佳那, 山元淳平, 岩井成憲, 菅澤薫, 胡桃坂仁志
    第47回日本分子生物学会年会, Nov. 2024, Japanese
    Oral presentation

  • ヌクレオチド除去修復のDNA損傷認識制御におけるヒストン修飾の役割
    綿田瑞希, 日下部将之, 前田拓海, 各務恵理菜, 横井雅幸, 酒井恒, 菅澤薫
    第47回日本分子生物学会年会, Nov. 2024, Japanese
    Poster presentation

  • 酸化的RNA損傷を鋳型としたSARS-CoV-2由来RNA依存性RNAポリメラーゼのRNA合成機構の解明
    赤川真崇, Grúz Petr, 菅澤薫, 浦聖恵, 佐々彰
    第47回日本分子生物学会年会, Nov. 2024, Japanese
    Poster presentation

  • アルデヒド脱水素酵素ALDH3A2の欠損がゲノム安定性に及ぼす影響
    䑺谷智也, 岡田太郎, 梶本武利, 篠原正和, 横井雅幸, 菅澤薫, 酒井恒
    第47回日本分子生物学会年会, Nov. 2024, Japanese
    Poster presentation

  • ヌクレオチド除去修復のDNA損傷認識を制御するクロマチン構造変換機構
    藤原叶枝, 槌田千輝, 日下部将之, 草尾佳那子, 八鍬聖, 横井雅幸, 酒井恒, 菅澤薫
    第47回日本分子生物学会年会, Nov. 2024, Japanese
    Poster presentation

  • Impacts of heavy water on DNA double-strand break repairs and cellular transcription, potentially via quantum-level mechanisms underlying kinetic isotope effects
    Yasuda Takeshi, Nakajima Nakako, Tomoo Ogi, Yanaka Tomoko, Tanaka Izumi, Gotoh Takaya, Wataru Kagawa, Kaoru Sugasawa, Tajima Katsushi
    The12th 3R+3C International Symposium, Nov. 2024, English
    Poster presentation

  • The involvement of chromatin remodeling factor SMACRAD1 in response to DNA double strand breaks
    Miou Takasu, Masayuki Kusanabe, Atsushi Shibata, Wataru Sakai, Kaoru Sugasawa, Masayuki Yokoi
    The12th 3R+3C International Symposium, Nov. 2024, English
    [Invited]
    Poster presentation

  • Impact of histone modifications on damage recognition process of global genome nucleotide excision repair
    Masayuki Kusakabe, Mizuki Watada, Takumi Maeda, Erina Kakumu, Kanae Fujiwara, Mizuki Otobe, Wataru Sakai, Masayuki Yokoi, Kaoru Sugasawa
    The12th 3R+3C International Symposium, Nov. 2024, English
    Poster presentation

  • Cryo-EM analyses of UV-damaged recognition protein UV-DDB in nucleosomes during nucleotide excision repair
    Syota Matsumoto, Yoshimasa Takizawa, Mitsuo Ogasawara, Kana Hashimoto, Junpei Yamamoto, Shigenori Iwai, Kaoru Sugasawa, Hitoshi Kurumizaka
    The12th 3R+3C International Symposium, Nov. 2024, English
    Poster presentation

  • Cooperation of Cdt2 C-terminal motifs in regulating CRL4Cdt2 dynamics at the DNA replication site
    Akiyo Hayashi, Tatsuya Bekki, Masayuki Kusanabe, Akiko Ueno, Yasushi Shiomi, Kaoru Sugasawa, Hideo Nishitani
    The12th 3R+3C International Symposium, Nov. 2024, English
    Poster presentation

  • Contribution of translesion synthesis for mutagenesis via a novel food-induced formamidopyrimidine-derivative
    Jun-ichi Akagi, Masayuki Yokoi, Kohei Matsushita, Fumio Hanaoka, Kaoru Sugasawa, Shigenori Iwai, Kumiko Ogawa
    The12th 3R+3C International Symposium, Nov. 2024, English
    Poster presentation

  • Effects of DNA substrate structures on lesion excision by nucleotide excision repair in vitro
    Hidetsugu Kozono, Hiroo Matsuyama, Haruto Tada, Masayuki Kusakabe, Syota Matsumoto, Tomoya Kujirai, Kenta Echigoya, Hitoshi Kurumizaka, Kaoru Sugasawa
    The12th 3R+3C International Symposium, Nov. 2024, English
    [Invited]
    Poster presentation

  • The agile dance of XP proteins in nucleotide excision repair
    Wei Yang, Jinseok Kim, Li Eric CL, Fumio Hanaoka, Kaoru Sugasawa
    The12th 3R+3C International Symposium, Nov. 2024, English
    [Invited]
    Invited oral presentation

  • Chromatin dynamics regulating DNA damage recognition for nucleotide excision repair
    Kaoru Sugasawa
    The12th 3R+3C International Symposium, Nov. 2024, English
    [Invited]
    Invited oral presentation

  • ヌクレオチド除去修復の損傷認識制御におけるヒストン修飾の役割
    日下部将之, 綿田瑞希, 前田拓海, 各務恵理菜, 藤原叶枝, 田口萌衣, 酒井恒, 横井雅幸, 菅澤薫
    日本放射線影響学会第67回大会, Sep. 2024, Japanese
    Oral presentation

  • ヌクレオチド除去修復におけるDNA損傷認識の制御機構
    古園英嗣, 松山宏生, 多田遥人, 日下部将之, 松本翔太, 鯨井智也, 越後谷健太, 胡桃坂仁志, 菅澤薫
    日本放射線影響学会第67回大会, Sep. 2024, Japanese
    Oral presentation

  • クライオ電子顕微鏡による細胞内クロマチン上のDNA損傷修復機構の理解
    松本翔太, 滝沢由政, 小笠原光雄, 橋本佳那, 山元淳平, 岩井成憲, 菅澤薫, 胡桃坂仁志
    日本放射線影響学会第67回大会, Sep. 2024, Japanese
    Oral presentation

  • 重水によるDNA二重鎖切断修復阻害は、加水分解酵素反応に対する量子レベルの速度論的同位体効果によると推測される
    安田 武嗣, 中島 菜花子, 谷中 智子, 後藤 孝也, 香川 亘, 菅澤 薫, 田嶋 克史
    日本放射線影響学会第67回大会, Sep. 2024, Japanese
    Oral presentation

  • アクリルアミドの活性代謝物であるグリシドアミドのホルムアミドピリミジン誘導体による突然変異誘発機序
    赤木純一, 横井雅幸, 三宅ゆみ, 白井剛, 馬場智弘, 曺永晩, 花岡文雄, 菅澤薫, 岩井成憲, 小川久美子
    第83回日本癌学会学術総会, Sep. 2024, Japanese
    Oral presentation

  • DNA修復の機能不全によるDNA鎖切断を伴わない自然免疫応答メカニズムの解明
    田中 陽菜, 山北 啓吾, 安井 学, 本間 正充, 杉山 圭一, 藤木 亮次, 金田 篤志, 菅澤 薫, 浦 聖恵, 佐々 彰
    第31回日本免疫毒性学会学術年会, Sep. 2024, Japanese
    Poster presentation

  • DNA鎖切断に起因するインターフェロン応答における核酸センサーcGAS,IFI16の役割
    寺越菜央, 山北啓吾, 安井学, 本間正充, 杉山圭一, 菅澤薫, 浦聖恵, 佐々彰
    第31回日本免疫毒性学会学術年会, Sep. 2024, Japanese
    Oral presentation

  • Uncovering distinct DNA damage responses associated with RNase H2 deficiency and its pathogenic mutation in human TK6 cells
    Kazuma Nakatani, Nao Terakoshi, Keigo Yamakita, Asuka Tachikawa, Hina Tanaka, Ayano Watanabe, Ken Takafuji, Yuiko Mayuzumi, Yui Yoshimoto, Takayuki Fukuda, Kaoru Sugasawa, Kiyoe Ura, Akira Sassa
    Gutenberg Workshop RNase H 2024: Structures, Functions and Disorders, Sep. 2024, English

  • In vitro RNA synthesis past oxidative base damage by SARS-CoV-2 RNA-dependent RNA polymerase
    Masataka Akagawa, Petr Grúz, Kaoru Sugasawa, Kiyoe Ura, Akira Sassa
    55th Annual Meeting of the EMGS, Sep. 2024, English
    Oral presentation

  • Contribution of translesion synthesis for mutagenesis via a novel food-induced formamidopyrimidine-derivative
    Jun-ichi Akagi, Masayuki Yokoi, Yumi Miyake, Tsuyoshi Shirai, Tomohiro Baba, Young-Man Cho, Fumio Hanaoka, Kaoru Sugasawa, Shigenori Iwai, Kumiko Ogawa
    7th DNA Polymerases Meeting, Aug. 2024, English
    Poster presentation

  • グリシドアミド付加体のホルムアミドピリミジン誘導体はDNA複製阻害と突然変異を誘発する
    赤木純一, 横井雅幸, 三宅ゆみ, 白井剛, 馬場智弘, 曺永晩, 花岡文雄, 菅澤薫, 岩井成憲, 小川久美子
    第51回日本毒性学会学術年会, Jul. 2024, Japanese
    Poster presentation

  • グリシドアミド付加体のホルムアミドピリミジン誘導体はDNA複製阻害と突然変異を誘発する
    赤木純一, 横井雅幸, 三宅ゆみ, 白井 剛, 馬場智弘, 曺 永晩, 花岡文雄, 菅澤 薫, 岩井成憲, 小川久美子
    日本薬学会年第144年会, Mar. 2024, Japanese
    Poster presentation

  • ヌクレオチド除去修復における損傷クロマチン認識機構の構造基盤と理解
    松本翔太, 滝沢由政, 小笠原光雄, 橋本佳那, 山元淳平, 岩井成憲, 菅澤 薫, 胡桃坂仁志
    第41回染色体ワークショップ・第22回核ダイナミクス研究会, Jan. 2024, Japanese
    Poster presentation

  • 損傷クロマチン基質を用いたヌクレオチド除去修復制御機構の生化学的解析
    古園英嗣, 多田遥人, 日下部将之, 松本翔太, 横井雅幸, 酒井 恒, 鯨井智也, 胡桃坂仁志, 菅澤 薫
    第41回染色体ワークショップ・第22回核ダイナミクス研究会, Jan. 2024, Japanese
    Poster presentation

  • ヌクレオチド除去修復の損傷監視制御におけるヒストン修飾の役割
    日下部将之, 綿田瑞希, 前田拓海, 各務恵理菜, 藤原叶枝, 乙部瑞貴, 酒井 恒, 横井雅幸, 菅澤 薫
    第41回染色体ワークショップ・第22回核ダイナミクス研究会, Jan. 2024, Japanese
    Oral presentation

  • 細胞の⽣存は量⼦効果に⽀配されている
    安田武嗣, 中島菜花子, 荻 朋男, 谷中智子, 田中 泉, 後藤孝也, 香川 亘, 菅澤 薫, 田嶋克史
    第46回日本分子生物学会年会, Dec. 2023, Japanese
    Poster presentation

  • ヌクレオチド除去修復のDNA損傷認識制御におけるヒストンH3K9メチル化修飾の役割
    綿田瑞希, 日下部将之, 前田拓海, 各務恵理菜, 横井雅幸, 酒井 恒, 菅澤 薫
    第46回日本分子生物学会年会, Dec. 2023, Japanese
    Poster presentation

  • 紫外線誘発DNA損傷に対する細胞応答におけるクロマチンリモデリング因⼦SMARCAD1の関与
    高須美央, 坂口友美, 酒井麻衣, 鹿谷有由希, 福永 匠, 酒井 恒, 日下部将之, 菅澤 薫, 花岡文雄, 横井雅幸
    第46回日本分子生物学会年会, Dec. 2023, Japanese
    Poster presentation

  • DNAポリメラーゼ‧イータの発現調節における脱ユビキチン化酵素USP11の関与
    中森晴渚, 仲野由佳梨, 案済 萌, 菅野新一郎, 安井 明, 酒井 恒, 菅澤 薫, 花岡文雄, 横井雅幸
    第46回日本分子生物学会年会, Dec. 2023, Japanese
    Poster presentation

  • ゲノム全体を対象としたヌクレオチド除去修復の損傷認識を制御するクロマチン動態
    日下部将之, 前田拓海, 綿田瑞希, 藤原叶枝, 各務恵理菜, 乙部瑞貴, 酒井 恒, 横井雅幸, 菅澤 薫
    第46回日本分子生物学会年会, Dec. 2023, Japanese
    Oral presentation

  • ⾷品汚染物質アクリルアミドの活性代謝物により⽣じるホルムアミドピリミジン誘導体の突然変異誘発機構
    赤木純一, 横井雅幸, 三宅ゆみ, 白井 剛, 馬場智弘, 曺 永晩, 花岡文雄, 菅澤 薫, 岩井成憲, 小川久美子
    第46回日本分子生物学会年会, Dec. 2023, Japanese
    Oral presentation

  • ヒストン翻訳後修飾を介したXPCタンパク質の核内局在制御
    乙部瑞貴, 日下部将之, 各務恵理菜, 槌田千輝, 塩月陽人, 酒井 恒, 横井雅幸, 菅澤 薫
    第46回日本分子生物学会年会, Dec. 2023, Japanese
    Poster presentation

  • ヌクレオチド除去修復のDNA損傷認識を制御するクロマチン構造変換機構
    藤原叶枝, 槌田千輝, 日下部将之, 草尾佳那子, 八鍬 聖, 酒井 恒, 横井雅幸, 菅澤 薫
    第46回日本分子生物学会年会, Dec. 2023, Japanese
    Poster presentation

  • DNA損傷を起因とした過剰なインターフェロン応答の分子経路の同定
    寺越 央, 高藤 賢, 中谷一真, 安井 学, 本間正充, 杉山圭一, 藤木亮次, 金田篤志, 菅澤 薫, 浦 聖恵, 佐々 彰
    日本環境変異原ゲノム学会第52回大会, Nov. 2023, Japanese
    Poster presentation

  • ゲノムDNAに蓄積したリボヌクレオチドが誘発するゲノム不安定化の分子機構
    立川明日香, 吉本侑依, 高藤 賢, 黛結衣子, 中谷一真, 中村真生, 福田隆之, 菅澤 薫, 浦 聖恵, 佐々 彰
    日本環境変異原ゲノム学会第52回大会, Nov. 2023, Japanese
    Poster presentation

  • SARS-CoV-2におけるRNA依存性RNAポリメラーゼの損傷乗り越えRNA合成機構の解析
    赤川真崇, Petr Grúz, 菅澤 薫, 浦 聖恵, 佐々 彰
    赤川真崇、Petr Grúz、菅澤 薫、浦 聖恵、佐々 彰, Nov. 2023, Japanese
    Poster presentation

  • 脂肪族アルデヒド脱水素酵素の欠損により生じる細胞毒性の解析
    䑺谷智也, 大槻侑恵, 後藤元成, 笹野真唯子, 松田 俊, 松田知成, 梶本武利, 岡田太郎, 横井雅幸, 菅澤 薫, 酒井 恒
    日本環境変異原ゲノム学会第52回大会, Nov. 2023, Japanese
    Poster presentation

  • 脂肪族アルデヒド脱水素酵素のゲノム安定性維持における影響
    酒井 恒, 䑺谷智也, 大槻侑恵, 後藤元成, 笹野真唯子, 松田 俊, 松田知成, 梶本武利, 岡田太郎, 横井雅幸, 菅澤 薫
    日本環境変異原ゲノム学会第52回大会, Nov. 2023, Japanese
    Oral presentation

  • クライオ電子顕微鏡による紫外線損傷修復機構の構造基盤の理解
    松本翔太, 滝沢由政, 小笠原光雄, 橋本佳那, 山元淳平, 岩井成憲, 菅澤 薫, 胡桃坂仁志
    日本放射線影響学会第66回大会, Nov. 2023, Japanese
    Oral presentation

  • ヌクレオチド除去修復の正確性を保証するDNA損傷認識の分子構造基盤
    菅澤 薫, 花岡文雄, Wei Yang
    日本放射線影響学会第66回大会, Nov. 2023, Japanese
    Oral presentation

  • ゲノム全体を対象としたヌクレオチド除去修復の損傷認識制御におけるヒストン修飾の役割
    日下部将之, 前田拓海, 綿田瑞希, 各務恵理菜, 乙部瑞貴, 藤原叶枝, 菅澤 薫
    日本放射線影響学会第66回大会, Nov. 2023, Japanese
    Oral presentation

  • 損傷クロマチン基質を用いたヌクレオチド除去修復制御機構の生化学的解析
    古園英嗣, 多田遥人, 日下部将之, 菅澤 薫
    日本遺伝学会第95回大会, Sep. 2023, Japanese
    Poster presentation

  • ヌクレオチド除去修復の正確性を保証するDNA損傷認識の分子構造基盤
    菅澤 薫, Jinseok Kim, Chia-Lung Li, uemin Chen, Yanxiang Cui, Filip, M. Golebiowski, Huaibin Wang, 花岡文雄, Wei Yang
    日本遺伝学会第95回大会, Sep. 2023, Japanese
    Oral presentation

  • ヌクレオチド除去修復の損傷認識制御におけるヒストン修復の役割
    日下部将之, 前田拓海, 綿田瑞希, 各務恵理菜, 菅澤 薫
    第27回DNA複製・組換え・修復ワークショップ, Jun. 2023, Japanese
    Oral presentation

  • 量子効果の想定外の大きな影響：細胞の生存は量子効果に支配されている
    安田 武嗣, 中島 菜花子, 荻 朋男, 谷中 智子, 後藤 孝也, 田中 泉, 香川 亘, 菅澤 薫, 田嶋 克史
    量子生命科学会第5回大会, May 2023, Japanese
    Poster presentation

  • Histone modifications regulating the initiation of global genome nucleotide excision repair
    Masayuki Kusakabe, Takumi Maeda, Erina Kakumu, Mizuki Watada, Kaoru Sugasawa
    The 19th Ataxia-Telangiectasia Workshop (ATW2023), Mar. 2023, English
    Poster presentation

  • 損傷クロマチン基質におけるヌクレオチド除去修復開始制御機構の解析
    古園英嗣, 多田遥人, 日下部将之, 菅澤 薫
    若手フロンティア研究会2022, Dec. 2022, Japanese
    Poster presentation

  • ヒストン修飾を介したヌクレオチド除去修復の損傷認識促進機構
    日下部将之, 前田拓海, 各務恵理菜, 綿田瑞希, 菅澤 薫
    第45回日本分子生物学会年会, Dec. 2022, Japanese
    Poster presentation

  • ヒストン修飾を介したヌクレオチド除去修復の損傷認識促進機構
    日下部将之, 前田拓海, 各務恵理菜, 綿田瑞希, 菅澤 薫
    第45回日本分子生物学会年会, Dec. 2022, Japanese
    Oral presentation

  • 脂質代謝制御におけるファンコニ貧血タンパク質の機能解析
    酒井 恒, 䑺谷智也, 大槻侑恵, 後藤元成, 乾 愛実, 松田 俊, 松田知成, 横井雅幸, 菅澤 薫
    第45回日本分子生物学会年会, Nov. 2022, Japanese
    Poster presentation

  • ヌクレオチド除去修復におけるDNA損傷認識を制御するクロマチン構造変換因子複合体
    槌田千輝, 日下部将之, 各務恵理菜, 栗原文佳, 草尾佳那子, 前田拓海, 横井雅幸, 酒井 恒, 菅澤 薫
    第45回日本分子生物学会年会, Nov. 2022, Japanese
    Poster presentation

  • 脂質代謝制御におけるファンコニ貧血タンパク質の機能解析
    酒井 恒, 䑺谷智也, 大槻侑恵, 後藤元成, 乾 愛実, 松田 俊, 松田知成, 横井雅幸, 菅澤 薫
    第45回日本分子生物学会年会, Nov. 2022, Japanese
    Oral presentation

  • Understanding the Molecular Mechanism of Innate Immune Response Caused by DNA Repair Deficiency
    高藤 賢, 岩崎 滉, 黛 結衣子, 立川明日香, 中谷一真, 安井 学, 本間正充, 杉山圭一, 藤木亮次, 金田篤志, 菅澤 薫, 浦 聖恵, 佐々 彰
    日本環境変異原ゲノム学会第51回大会, Nov. 2022, Japanese
    Poster presentation

  • γH2AXの多角的解析による内因性DNA二本鎖切断の定量評価
    立川明日香, 吉本侑依, 高藤 賢, 黛 結衣子, 中谷一真, 中村真生, 福田隆之, 菅澤 薫, 浦 聖恵, 佐々 彰
    日本環境変異原ゲノム学会第51回大会, Nov. 2022, Japanese
    Poster presentation

  • ゲノム中リボヌクレオチドの蓄積が誘発するDNA二本鎖切断の修復機構
    黛 結衣子, 高藤 賢, 立川明日香, 中谷一真, 安井 学, 本間正充, 杉山圭一, 菅澤 薫, 浦 聖恵, 佐々 彰
    日本環境変異原ゲノム学会第51回大会, Nov. 2022, Japanese
    Poster presentation

  • Ring-Opened N7-deoxyguanosine adduct of glycidamide induces DNA replication inhibition and mutagenesis
    Jun-ichi Akagi, Masayuki Yokoi, Young-Man Cho, Fumio Hanaoka, KaoruSugasawa, Shigenori Iwai, Kumiko Ogawa
    第49回国際核酸化学シンポジウム, Nov. 2022, English
    Poster presentation

  • Roles of histone modifications in DNA damage recognition initiating global genome nucleotide excision repair
    Masayuki Kusakabe, Takumi Maeda, Erina Kakumu, Mizuki Watada, Kaoru Sugasawa
    2022 International IBS Conference for Genomic Integrity, Oct. 2022, English
    Poster presentation

  • Chromatin dynamics regulating initiation of nucleotide excision repair
    Masayuki Kusakabe, Erina Kakumu, Fumika Kurihara, Kazuki Tsuchida, Takumi Maeda, Mizuki Otobe, Kaoru Sugasawa
    2022 International IBS Conference for Genomic Integrity, Oct. 2022, English
    [Invited]
    Invited oral presentation

  • Chromatin dynamics regulating initiation of nucleotide excision repair
    Masayuki Kusakabe, Kaoru Sugasawa
    International Conference of the Genetics Society of Korea 2022 (ICGSK2022), Oct. 2022, English
    [Invited]
    Invited oral presentation

  • Roles of histone modifications in DNA damage recognition initiating global genome nucleotide excision repair
    Masayuki Kusakabe, Takumi Maeda, Erina Kakumu, Mizuki Watada, Kaoru Sugasawa
    International Conference of the Genetics Society of Korea 2022 (ICGSK2022), Oct. 2022, English
    Poster presentation

  • ヌクレオチド除去修復における紫外線誘発DNA損傷の効率的な認識に寄与するヒストン修飾
    日下部将之, 前田拓海, 各務恵理菜, 綿田瑞希, 酒井 恒, 横井雅幸, 菅澤 薫
    日本放射線影響学会第65回大会, Sep. 2022, Japanese
    Oral presentation

  • 損傷乗り越え型DNAポリメラーゼPolκとREV1はグリシドアミドN7位デオキシグアノシン付加体による点突然変異に寄与する
    赤木純一, 横井雅幸, Young-Man Cho, 岩井成憲, 花岡文雄, 菅澤薫, 小川久美子
    日本薬学会第142年会, Mar. 2022, Japanese
    Poster presentation

  • 色素性乾皮症C群タンパク質によるDNA損傷認識を制御するクロマチン動態
    前田拓海, 日下部将之, 横井雅幸, 酒井恒, 菅澤薫
    第39回染色体ワークショップ・第20回核ダイナミクス研究会, Dec. 2021, Japanese
    Poster presentation

  • ヒストン脱アセチル化はヌクレオチド除去修復におけるDNA損傷認識を制御する
    槌田千輝, 日下部将之, 各務恵理菜, 栗原文佳, 多田遥人, 前田拓海, 横井雅幸, 酒井恒, 菅澤薫
    第39回染色体ワークショップ・第20回核ダイナミクス研究会, Dec. 2021, Japanese
    Poster presentation

  • ヒストン脱アセチル化はヌクレオチド除去修復におけるDNA損傷認識を制御する
    槌田千輝, 日下部将之, 各務恵理菜, 栗原文佳, 多田遥人, 前田拓海, 横井雅幸, 酒井 恒, 菅澤 薫
    第44回日本分子生物学会年会, Dec. 2021, Japanese
    Poster presentation

  • 脱ユビキチン化酵素による損傷乗り越え合成の制御機構の解析
    仲野由佳梨, 案済萌, 菅野新一郎, 安井明, 酒井恒, 菅澤薫, 花岡文雄, 横井雅幸
    第44回日本分子生物学会年会, Dec. 2021, Japanese
    Poster presentation

  • ファンコニ貧血タンパク質の脂質代謝における機能解析
    䑺谷智也, 大槻侑恵, 後藤元成, 乾 愛実, 横井雅幸, 菅澤 薫, 酒井 恒
    第44回日本分子生物学会年会, Dec. 2021, Japanese
    Poster presentation

  • 色素性乾皮症C群タンパク質によるDNA損傷認識を制御するクロマチン動態
    前田拓海, 日下部将之, 横井雅幸, 酒井 恒, 菅澤 薫
    第44回日本分子生物学会年会, Dec. 2021, Japanese
    Poster presentation

  • グリシドアミドN7位デオキシグアノシン付加体による点突然変異に寄与する損傷乗り越え型DNAポリメラーゼの解析
    赤木 純一, 横井 雅幸, Young-Man Ch, 岩井 成憲, 森谷 正明, 花岡 文雄, 菅澤 薫, 小川 久美子
    第44回日本分子生物学会年会, Dec. 2021, Japanese
    Oral presentation

  • DNA損傷修復において機能するCRL4ユビキチンリガーゼの損傷部位集積機構のライブイメージ解析
    海老原 渓, 日下部将之, 林 晃世, 塩見泰史, 菅澤 薫, 西谷秀男
    第44回日本分子生物学会年会, Dec. 2021, Japanese
    Poster presentation

  • ヌクレオチド除去修復におけるDNA損傷認識を制御するクロマチンダイナミクス
    日下部将之, 各務恵理菜, 栗原文佳, 槌田千輝, 多田遥人, 横井雅幸, 酒井 恒, 菅澤 薫
    第94回日本生化学会大会, Nov. 2021, Japanese
    Oral presentation

  • ゲノム安定性維持に関わるCRL4Cdt2ユビキチンリガーゼの損傷部位集積機構の解析
    海老原渓, 日下部将之, 林 晃世, 塩見泰史, 菅澤 薫, 西谷秀男
    第26回DNA複製・組換え・修復ワークショップ, Oct. 2021, Japanese
    Oral presentation

  • 紫外線誘発DNA損傷の効率的な認識と修復を保障するヒストン修飾の役割
    日下部将之, 各務恵理菜, 栗原文佳, 槌田千輝, 多田遥人, 前田拓海, 菅澤薫
    日本放射線影響学会第 64 回大会, Sep. 2021, Japanese
    Oral presentation

  • ヌクレオチド除去修復の損傷認識を補助するクロマチン構造変換機構の解明
    前田拓海, 日下部将之, 菅澤薫
    日本遺伝学会第93回大会, Sep. 2021, Japanese
    Oral presentation

  • 光刺激を用いたゲノムDNA損傷応答の研究
    菅澤 薫
    第1回広帯域極限電磁波生命理工連携研究会, Sep. 2021, Japanese
    [Invited]
    Invited oral presentation

  • A new regulatory mechanism of chromatin dynamics triggered by DNA damage recognition protein DDB2
    Syota Matsumoto, Simone Cavadini, Richard D. Bunker, Ralph S. Grand, Junpei Yamamoto, Dirk Schübeler, Shigenori Iwai, Kaoru Sugasawa, Hitoshi Kurumizaka, Nicolas H. Thomä
    第43回日本分子生物学会年会, Dec. 2020, Japanese
    Poster presentation

  • Tyrosyl-DNA phosphodiesterasesはDNA中のリボヌクレオチドを起因とする突然変異形成に関与する
    竹石 歩奈, 古樫 浩之, 小田切 瑞基, 笹沼 博之, 武田 俊一, 安井 学, 本間 正充, 菅澤 薫, 浦 聖恵, 佐々 彰
    第43回日本分子生物学会年会, Dec. 2020, Japanese
    Poster presentation

  • 脂質代謝におけるファンコニ貧血タンパク質の機能解析
    酒井恒, 大槻侑恵, 後藤元成, 乾愛実, 䑺谷智也, 横井雅幸, 菅澤薫
    日本環境変異原学会第49回大会, Nov. 2020, Japanese
    Oral presentation

  • 色素性乾皮症タンパク質による紫外線誘発DNA損傷認識の生体内制御機構
    菅澤薫
    日本遺伝学会第92回大会, Sep. 2020, Japanese
    Oral presentation

  • The N7-glycidamide adduct of 2’-deoxyguanosine on the template strand induces DNA replication inhibition and mutagenesis in human cells
    Jun-ichi Akagi, Masayuki Yokoi, Young-Man Cho, Shigenori Iwai, Fumio Hanaoka, Kaoru Sugasawa, Kumiko Ogawa
    第47回日本毒性学会学術年会, Jun. 2020, English
    Poster presentation

  • Functional analysis of histone modifications regulating recognition of DNA lesions in nucleotide excision repair.
    Masayuki Kusakabe, Takumi Maeda, Kanako Kusao, Fumika Kurihara, Erina Kakumu, Kaoru Sugasawa
    4th DNA Repair/Replication Structures and Cancer Conference, English
    Poster presentation

  • ヌクレオソーム上における DNAスライドを介した新たな紫外線損傷認識メカニズムの解明
    松本翔太, Simone Cavadini, Richard Bunker, Ralph Grand, Alessandro Potenza, Julius Rabl, 山元淳平, Andreas Schenk, Dirk Schuebeler, 岩井成憲, 菅澤 薫, 胡桃坂仁志, Nicolas Thomae
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • N7-グリシドアミドdG付加体により誘発されるDNA複製阻害と変異原性の解析
    赤木純一, 横井雅幸, Young-Man Cho, 岩井成憲, 花岡文雄, 菅澤 薫, 小川久美子
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • RNAを介したヌクレオチド除去修復制御機構の解析
    古川真理, 日下部将之, 酒井 恒, 横井雅幸, 菅澤 薫
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • 脂質代謝に応答したファンコニ貧血タンパク質のダイナミクス
    酒井 恒, 乾 愛実, 大槻侑恵, 後藤元成, 横井雅幸, 菅澤 薫
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • ファンコニ貧血タンパク質FANCD2と脂質代謝関連因子の機能的連関の解析
    大槻侑恵, 後藤元成, 乾 愛実, 松田 俊, 松田知成, 横井雅幸, 菅澤 薫, 酒井 恒
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • DNAポリメラーゼ・イータと脱ユビキチン化酵素の相互作用の解析
    案済 萌, 西村 潤, 菅野新一郎, 安井 明, 酒井 恒, 菅澤 薫, 花岡文雄, 横井雅幸
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • TLSポリメラーゼの損傷部位への導入過程を生細胞イメージングにより解 析する試み
    福永 匠, 尾崎未羽, 佐藤正康, 酒井 恒, 菅澤 薫, 花岡文雄, 横井雅幸
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • XPCタンパク質によるDNA損傷認識の制御とヒストン修飾の役割
    栗原文佳, 日下部将之, 各務恵理菜, 草尾佳那子, 前田拓海, 横井雅幸, 酒井 恒, 菅澤 薫
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • ヌクレオチド除去修復の損傷認識を制御するクロマチン構造変換因子の探 索
    草尾佳那子, 日下部将之, 各務恵理菜, 栗原文佳, 前田拓海, 横井雅幸, 酒井 恒, 菅澤 薫
    第42回日本分子生物学会年会, Japanese
    Poster presentation

  • ゲノムの安定維持を保証するDNA損傷認識の高次制御機構
    菅澤 薫
    金沢大学薬学シンポジウム2019「多様な生体防御システム研究のイノベーション〜アンメット・メディカル・ニーズから創薬へ〜」, Nov. 2019, Japanese
    [Invited]
    Invited oral presentation

  • Mechanistic insight of unique mutations caused by a ribonucleotide embedded into DNA.
    Ayuna Takeishi, Manabu Yasui, Hiroyuki Sasanuma, Shunichi Takeda, Kaoru Sugasawa, Masamitsu Honma, Kiyoe Ura, Akira Sassa
    6th Asian Congress on Environmental Mutagens (ACEM) and 48th Annual Meeting of the Japanese Environmental Mutagen Society (JEMS), English
    Poster presentation

  • Alternate processing pathways of a single ribonucleotide incorporated into DNA and its consequences in human cells.
    Akira Sassa, Haruto Tada, Ayuna Takeishi, Kaho Harada, Kazuma Nakatani, Masataka Tsuda, Hiroyuki Sasanuma, Shunichi Takeda, Kaoru Sugasawa, Manabu Yasui, Masamitsu Honma, Kiyoe Ura
    6th Asian Congress on Environmental Mutagens (ACEM) and 48th Annual Meeting of the Japanese Environmental Mutagen Society (JEMS), English
    Oral presentation

  • Chromatin dynamics regulating DNA lesion recognition in nucleotide excision repair
    Masayuki Kusakabe, Fumika Kurihara, Kanako Kusao, Masayuki Yokoi, Wataru Sakai, Kaoru Sugasawa
    6th Asian Congress on Environmental Mutagens (ACEM) and 48th Annual Meeting of the Japanese Environmental Mutagen Society (JEMS), English
    Oral presentation

  • Functional analysis of histone modifications regulating recognition of UV-induced DNA lesions in nucleotide excision repair.
    Masayuki Kusakabe, Erina Kakumu, Manami Kobayashi, Kaoru Sugasawa
    日本放射線影響学会第62回大会, English
    Oral presentation

  • Roles for ATPase activities of transcription factor IIH in nucleotide excision repair.
    Haruto Tada, Yuki Onishi, Shigenori Iwai, Kaoru Sugasawa
    Symposium of the Biosignal Research Center and the KAITAKU Project "Genome Function in Higher-Order Life Phenomena", Kobe University), Nov. 2019, English
    Oral presentation

  • Functional analysis of chromatin remodeling machinery regulating recognition of DNA lesions in nucleotide excision repair.
    Masayuki Kusakabe, Takumi Maeda, Erina Kakumu, Kaoru Sugasawa
    International Symposium on "Maintenance of Genome Integrity" (Joint Symposium of the Biosignal Research Center and the KAITAKU Project "Genome Function in Higher-Order Life Phenomena", Kobe University), Nov. 2019, English
    Oral presentation

  • ヌクレオチド除去修復の損傷認識を制御するヒストン修飾の解析
    日下部将之, 前田拓海, 各務恵理菜, 菅澤 薫
    第25回DNA複製・組換え・修復ワークショップ, Japanese
    Oral presentation

  • TLSポリメラーゼの生細胞イメージングとその定量解析への取り組み
    福永 匠, 酒井 恒, 菅澤 薫, 横井雅幸
    サイエンスフロンティア研究発表会, Oct. 2019, Japanese
    Poster presentation

  • Molecular mechanism of recognition and repair of UV-induced DNA damage.
    Kaoru Sugasawa
    9th Asia and Oceania Conference on Photobiology, English
    [Invited]
    Keynote oral presentation

  • Dynamics of FANCD2 in response to lipid metabolism.
    Yukie Otsuki, Motonari Goto, Megumi Inui, Masayuki Yokoi, Kaoru Sugasawa, Wataru Sakai
    2019 Fanconi Anemia Scientific Symposium, English
    Poster presentation

  • Chromatin dynamics regulating recognition of UV-induced DNA photolesions.
    Kaoru Sugasawa
    17th International Congress on Photobiology and 18th Congress of the European Society for Photobiology, English
    Oral presentation

  • 皮膚老化メカニズムの解明とその応用
    近藤可奈子, 菊永佐紀子, 山之上稔, 上田修司, 菅澤 薫, 白井康仁
    第135回日本薬理学会近畿部会, Jun. 2019, Japanese
    Poster presentation

  • In vivo regulation of DNA damage recognition for nucleotide excision repair
    Kaoru Sugasawa
    International Symposium on XP and other Nucleotide Excision Repair Disorders, Mar. 2019, English, Cambridge, U.K., International conference
    [Invited]
    Invited oral presentation

  • 脂肪族アルデヒド代謝におけるファンコニ貧血タンパク質の機能解析
    酒井 恒, 大槻侑恵, 後藤元成, 乾 愛実, 松田 俊, 松田知成, 菅澤 薫
    日本環境変異原学会第47回大会, Nov. 2018, Japanese, 京都, Domestic conference
    Oral presentation

  • 紫外線誘発DNA損傷修復の高次制御機構
    菅澤 薫
    日本放射線影響学会第61回大会, Nov. 2018, Japanese, 長崎, Domestic conference
    Oral presentation

  • ファンコニ貧血タンパク質FANCD2と脂質代謝関連因子の相互作用解析
    大槻侑恵, 後藤元成, 乾 愛実, 松田 俊, 松田 知成, 菅澤 薫, 酒井 恒
    第41回日本分子生物学会年会, Nov. 2018, Japanese, 横浜, Domestic conference
    Poster presentation

  • XPCタンパク質によるDNA損傷認識の制御におけるヒストン修飾の役割
    KURIHARA FUMIKA, KUSAKABE MASAYUKI, KATO AKARI, KAKUMU ERINA, NAKANISHI SEIYA, KUSAO KANAKO, OKAWA YASUYUKI, YOKOI MASAYUKI, SAKAI WATARU, SUGASAWA KAORU
    第41回日本分子生物学会年会, Nov. 2018, Japanese, 横浜, Domestic conference
    Poster presentation

  • Translesion synthesis-associated chromatin remodeling factors contribute the function of human DNA polymerase η in cisplatin-treated cells.
    Masayuki Yokoi, Yuuki Shikaya, Kaoru Sugasawa, Fumio Hanaoka
    The 11th 3R&3C Symposium, Nov. 2018, English, Kanazawa Japan, International conference
    Oral presentation

  • Functional analysis of histone modification in DNA damage recognition process of nucleotide excision repair.
    Masayuki Kusakabe, Fumika Kurihara, Akari Kato, Erina Kakumu, Manami Kobayashi, Kaoru Sugasawa
    The 11th 3R&3C Symposium, Nov. 2018, English, Kanazawa Japan, International conference
    Oral presentation

  • DNA中のリボヌクレオチドが引き起こす特異な突然変異とその誘発機構の 解析
    竹石歩奈, 安井 学, 笹沼 博之, 武田俊一, 菅澤 薫, 本間正充, 浦 聖恵, 佐々 彰
    日本環境変異原学会第47回大会, Nov. 2018, Japanese, 京都, Domestic conference
    Poster presentation

  • DNAポリメラーゼ・イータと脱ユビキチン化酵素の相互作用の解析
    案済 萌, 西村 潤, 菅野新一郎, 安井 明, 菅澤 薫, 花岡文雄, 横井雅幸
    第41回日本分子生物学会年会, Nov. 2018, Japanese, 横浜, Domestic conference
    Poster presentation

  • リボヌクレオチドが誘発する奇異突然変異とその防御機構
    佐々 彰, 安井 学, 竹石歩奈, 原田佳歩, 鈴木 慈, 津田雅貴, 笹沼博之, 武田俊一, 菅澤 薫, 本間正充, 浦 聖恵
    日本遺伝学会第90回大会, Sep. 2018, Japanese, 奈良, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復の損傷認識を制御するクロマチン構造変換機構の解明
    日下部将之, 各務恵理菜, 小林真奈美, 菅澤 薫
    第91回日本生化学会大会, Sep. 2018, Japanese, 京都, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復のDNA損傷認識を制御するクロマチン構造動態
    菅澤 薫
    第91回日本生化学会大会, Sep. 2018, Japanese, 京都, Domestic conference
    Oral presentation

  • クロマチン構造を介したヌクレオチド除去修復の高次制御機構
    日下部将之, 各務恵理菜, 加藤安佳梨, 栗原文佳, 草尾佳那子, 横井雅幸, 酒井 恒, SUGASAWA KAORU
    第91回生化学会大会, Sep. 2018, Japanese, 京都, Domestic conference
    Oral presentation

  • Functional impact of ubiquitin-proteasome system on UV-induced DNA damage response and repair
    酒井 恒, 岸本 藍子, 金子 雄貴, 松井 豪志, 赤木 純一, 菅澤 薫
    日本遺伝学会第90回大会, Sep. 2018, Japanese, 奈良, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復におけるDNA損傷認識の高次制御機構
    SUGASAWA Kaoru
    日本薬学会第138年会, Mar. 2018, Japanese, 石川県立音楽堂他全9会場, Domestic conference
    Oral presentation

  • Coordinated DNA damage recognition by xeroderma pigmentosum gene products
    SUGASAWA Kaoru
    International Meeting on RECQ Helicases and Related Diseases 2018, Feb. 2018, English, かずさアカデミアパーク, International conference
    [Invited]
    Invited oral presentation

  • ヌクレオチド除去修復の開始を制御するクロマチン構造の役割
    KATO Akari, KAKUMU Erina, NAKANISHI Seiya, KUSAKABE Masayuki, KURIHARA Fumika, SAKAI Wataru, SUGASAWA Kaoru
    2017年度生命科学系学会合同年次大会, Dec. 2017, Japanese, 神戸国際会議場, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復における損傷認識機構の解析
    TADA Haruto, ONISHI Yuki, IWAI Shigenori, SUGASAWA Kaoru
    2017年度生命科学系学会合同年次大会, Dec. 2017, Japanese, 神戸国際会議場, Domestic conference
    Poster presentation

  • 脂質アルデヒド代謝におけるファンコニ貧血タンパク質の機能解析
    SAKAI Wataru, GOTO Motonari, OTSUKI Yukie, MATSUDA Shun, MATSUDA Tomonari, SUGASAWA Kaoru
    日本環境変異原学会第46回大会, Nov. 2017, Japanese, 一橋大学 一橋講堂, Domestic conference
    Poster presentation

  • ユビキチン-プロテアソーム系による紫外線誘発DNA損傷応答制御
    SAKAI Wataru, KISHIMOTO Aiko, KANEKO Yuki, MATSUI Takeshi, AKAGI Junichi, SUGASAWA Kaoru
    第24回DNA複製・組換え・修復ワークショップ, Nov. 2017, Japanese, 長良川国際会議場, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復の開始を制御するクロマチン構造の役割
    KATO Akari, KAKUMU Erina, NAKANISHI Seiya, KUSAKABE Masayuki, KURIHARA Fumika, SAKAI Wataru, SUGASAWA Kaoru
    第24回DNA複製・組換え・修復ワークショップ, Nov. 2017, Japanese, 長良川国際会議場, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復におけるDNA損傷認識機構の解析
    TADA Haruto, IWAI Shigenori, SUGASAWA Kaoru
    第24回DNA複製・組換え・修復ワークショップ, Nov. 2017, Japanese, 長良川国際会議場, Domestic conference
    Oral presentation

  • シスプラチン誘発DNA鎖内架橋の乗り越え合成に関わるヒストン修飾とクロマチン構造変換因子の探索
    YOKOI MASAYUKI, SHIKAYA YUUKI, SUGASAWA KAORU, 花岡 文雄
    第24回 DNA複製・組換え・修復ワークショップ, Nov. 2017, Japanese, 長良川国際会議場, Domestic conference
    Poster presentation

  • Mechanism and regulation of DNA damage recognition in nucleotide excision repair
    SUGASAWA Kaoru
    The 2nd Biosignal Research Center International Symposium, Nov. 2017, English, Kobe University, International conference
    Oral presentation

  • Chromatin dynamics regulating DNA damage recognition of nucleotide excision repair
    SUGASAWA Kaoru
    ICEM-ACEM 2017, Nov. 2017, English, Songdo Convensia/Seoul South Korea, International conference
    [Invited]
    Invited oral presentation

  • Fatty aldehyde dehydrogenase as a novel binding partner of FANCD2
    SAKAI Wataru, GOTO Motonari, OTSUKI Yukie, MATSUDA Shun, MATSUDA Tomonari, SUGASAWA Kaoru
    2017 FA Scientific Symposium, Sep. 2017, English, Grand Hyatt Atlanta in Buckhead/Atlanta USA, International conference
    [Invited]
    Invited oral presentation

  • Chromatin remodeling factors contribute to the function of human DNA polymerase η in the cells treated with cisplatin
    YOKOI MASAYUKI, SUGASAWA KAORU, HANAOKA FUMIO
    第76回 日本癌学会, Sep. 2017, Japanese, パシフィコ横浜, Domestic conference
    Poster presentation

  • Interaction of DNA damage recognition factors with chromatin.
    SUGASAWA Kaoru
    6th US-Japan DNA Repair Meeting, May 2017, English, Berkeley University of California/ Berkeley, USA, International conference
    [Invited]
    Invited oral presentation

  • 紫外線DNA損傷修復の分子機構
    SUGASAWA KAORU
    第27回太陽紫外線防御研究委員会シンポジウム, Mar. 2017, Japanese, 太陽紫外線防御研究委員会, 大阪, Domestic conference
    [Invited]
    Invited oral presentation

  • Interaction of DNA damage recognition factors with the chromatin structure
    Kaoru Sugasawa
    Japan-Swiss Symposium on Chromatin Structure and Dynamics, Jan. 2017, English, Basel, Switzerland, International conference
    Oral presentation

  • タンパク質分解系による紫外線誘発DNA損傷応答制御
    SAKAI WATARU, 岸本 藍子, 金子 雄貴, 松井 豪志, 赤木 純一, SUGASAWA KAORU
    第39回日本分子生物学会年会（MBSJ2016）, Nov. 2016, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Poster presentation

  • Roles of DNA topology and TFIIH ATPases in mammalian nucleotide excision repair
    Kaoru Sugasawa, Haruto Tada, Yuki Onishi, Chia-Lung Li, Filip M. Golebiowski, Wei Yang
    The 10th 3R Symposium, Nov. 2016, English, The 10th 3R Symposium Organizing Committee, Matsue, Shimane, Japan, International conference
    Oral presentation

  • Molecular mechanism ensuring accuracy of the nucleotide excision repair system
    Kaoru Sugasawa
    第39回日本分子生物学会年会（MBSJ2016), Nov. 2016, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Oral presentation

  • Functional impact of ubiquitin-proteasome system on UV-induced DNA damage response and repair
    Wataru Sakai, Aiko Kishimoto, Yuki Kaneko, Takeshi Matsui, Jun-ichi Akagi, Kaoru Sugasawa
    The 10th 3R Symposium, Nov. 2016, English, The 10th 3R Symposium Organizing Committee, Matsue, Shimane, Japan, International conference
    Poster presentation

  • FANCD2新規相互作用因子の探索と機能解析
    GOTO MOTONARI, 松田 俊, 松田 知成, SUGASAWA KAORU, SAKAI WATARU
    第39回日本分子生物学会年会（MBSJ2016）, Nov. 2016, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Oral presentation

  • DNA損傷認識を制御するクロマチン構造動態
    KAKUMU ERINA, 中西 正哉, SAKAI WATARU, ADACHI NAOKO, SAITO NAOAKI, 森 俊雄, 木村 宏, 胡桃坂 仁志, SUGASAWA KAORU
    第39回日本分子生物学会年会（MBSJ2016）, Nov. 2016, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Poster presentation

  • DNAのトポロジー状態がヌクレオチド除去修復に及ぼす影響
    TADA HARUTO, 大西 優貴, 岩井 成憲, SUGASAWA KAORU
    第39回日本分子生物学会年会（MBSJ2016）, Nov. 2016, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復のDNA損傷認識とその制御の分子基盤
    SUGASAWA KAORU, HARUTO TADA, 大西 優貴, 岩井成憲, 胡桃坂仁志, SAKAI WATARU
    第89回日本生化学会大会, Sep. 2016, Japanese, 日本分子生物学会, 仙台, Domestic conference
    Oral presentation

  • Studies on nucleotide excision repair：beginning with XPC and beyond
    Kaoru Sugasawa
    Symposium: Celebration Jan Hoeijmakers, Sep. 2016, English, Rotterdam, The Netherlands, International conference
    [Invited]
    Invited oral presentation

  • DNA damage recognition mechanism for mammalian nucleotide excision repair
    Kaoru Sugasawa
    KSBMB (Korean Society for Biochemistry and Molecular Biology) International Conference 2016, May 2016, English, KSBMB, Seoul, Korea, International conference
    [Invited]
    Invited oral presentation

  • Dynamics of chromatin structure regulating nucleotide excision repair
    Erina Kakumu, Seiya Nakanishi, Wataru Sakai, Naoko Adachi, Naoaki Saito, Hiroshi Kimura, Kaoru Sugasawa
    Conference on Responses to DNA Damage: from Molecule to Disease, Apr. 2016, English, Egmond aan Zee, The Netherlands, International conference
    Poster presentation

  • Dissection of the DNA damage recognition machinery in mammalian nucleotide excision repair
    Kaoru Sugasawa
    Conference on Responses to DNA Damage: from Molecule to Disease, Apr. 2016, English, Egmond aan Zee, The Netherlands, International conference
    [Invited]
    Invited oral presentation

  • 3R研究の今後の動向について
    Sugasawa Kaoru
    第13回SUMO研究会, Jan. 2016, Japanese, SUMO研究会, 大阪, Domestic conference
    Oral presentation

  • 3R研究の今後の動向について
    菅澤 薫
    第13回SUMO研究会, Jan. 2016, Japanese, SUMO研究会, 大阪, Domestic conference
    Oral presentation

  • 酸化的DNA/RNA脱メチル化酵素ALKBH3の機能解析
    稲瀬安希, 太田奈緒, 本橋ほづみ, Sugasawa Kaoru
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • 酸化的DNA/RNA脱メチル化酵素ALKBH3の機能解析
    稲瀬 安希, 太田 奈緒, 本橋 ほづみ, 菅澤 薫
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • 塩基除去修復因子チミンDNAグリコシラーゼの構造活性相関と機能制御
    中村知史, 村上浩一, 松田 俊, 松田知成, 上原芳彦, 小野哲也, 西谷秀男, Sugasawa Kaoru
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • 塩基除去修復因子チミンDNAグリコシラーゼの構造活性相関と機能制御
    中村 知史, 村上 浩一, 松田 俊, 松田 知成, 上原 芳彦, 小野 哲也, 西谷 秀男, 菅澤 薫
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ヒトメディエーター複合体hMED17サブユニットによる転写制御とDNA損傷修復機能の解明
    菊池祐子, 西谷紗織, 梅村啓靖, 田中亜紀, 廣瀬 豊, Sugasawa Kaoru, 大熊芳明
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ヒトメディエーター複合体hMED17サブユニットによる転写制御とDNA損傷修復機能の解明
    菊池 祐子, 西谷 紗織, 梅村 啓靖, 田中 亜紀, 廣瀬 豊, 菅澤 薫, 大熊 芳明
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ヒトRAD52のアセチル化を介した相同組換えにおけるアセチル化および脱アセチル化酵素の新規機能の解明
    安田武嗣, 香川 亘, 荻 朋男, 齋藤健吾, 加藤宝光, 鈴木健祐, 堂前 直, 滝澤和也, 早乙女(中邑)愛, 中沢由華, Matthew D, Genet, 宇井彩子, 花岡文雄, Sugasawa Kaoru, 岡安隆一, Penny A, Jeggo, 胡桃坂仁志, 田嶋克史
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Oral presentation

  • ヒトRAD52のアセチル化を介した相同組換えにおけるアセチル化および脱アセチル化酵素の新規機能の解明
    安田 武嗣, 香川 亘, 荻 朋男, 齋藤 健吾, 加藤 宝光, 鈴木 健祐, 堂前 直, 滝澤 和也, 早乙女(中邑) 愛, 中沢 由華, Matthew D, Genet, 宇井 彩子, 花岡 文雄, 菅 澤 薫, 岡安 隆一, Penny A, Jeggo, 胡桃坂 仁志, 田嶋 克史
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復を制御するタンパク質リン酸化の解析
    木下 実, 戸根大輔, 岩井成憲, Sugasawa Kaoru
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復を制御するタンパク質リン酸化の解析
    木下 実, 戸根 大輔, 岩井 成憲, 菅澤 薫
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復を制御するクロマチン構造動態の解析
    各務恵理菜, 中西正哉, 酒井 恒, Adachi Naoko, Saito Naoaki, 田嶋正二, Sugasawa Kaoru
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復を制御するクロマチン構造動態の解析
    各務 恵理菜, 中西 正哉, 酒井 恒, ADACHI NAOKO, SAITO NAOAKI, 田嶋 正二, 菅澤 薫
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復の細胞内制御機構とその多様性
    Sugasawa Kaoru
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復の細胞内制御機構とその多様性
    菅澤 薫
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Oral presentation

  • タンパク質分解系による紫外線損傷応答制御
    酒井 恒, 岸本藍子, 松井豪志, 金子雄貴, 赤木純一, Sugasawa Kaoru
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Oral presentation

  • タンパク質分解系による紫外線損傷応答制御
    酒井 恒, 岸本 藍子, 松井 豪志, 金子 雄貴, 赤木 純一, 菅澤 薫
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Oral presentation

  • ゲノム損傷応答におけるp53とDDB2の機能連関
    上村美花, 松本翔太, 安田武嗣, 酒井 恒, Sugasawa Kaoru
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会（BMB2015）, Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ゲノム損傷応答におけるp53とDDB2の機能連関
    上村 美花, 松本 翔太, 安田 武嗣, 酒井 恒, 菅澤 薫
    第38回日本分子生物学会年会・第88回日本生化学会大会合同大会(BMB2015), Dec. 2015, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • 紫外線誘発DNA損傷の修復促進と皮膚癌の抑制に関わる分子機構
    Sugasawa Kaoru
    第74回日本癌学会学術総会, Oct. 2015, Japanese, 日本癌学会, 名古屋, Domestic conference
    Oral presentation

  • 紫外線誘発DNA損傷の修復促進と皮膚癌の抑制に関わる分子機構
    菅澤 薫
    第74回日本癌学会学術総会, Oct. 2015, Japanese, 日本癌学会, 名古屋, Domestic conference
    Oral presentation

  • 酸化的DNA/RNA脱メチル化酵素ALKBH3の発現変化は細胞増殖や代謝に影響を与える
    稲瀬安希, 本橋ほづみ, Sugasawa Kaoru
    第74回日本癌学会学術総会, Oct. 2015, Japanese, 日本癌学会, 名古屋, Domestic conference
    Poster presentation

  • 酸化的DNA/RNA脱メチル化酵素ALKBH3の発現変化は細胞増殖や代謝に影響を与える
    稲瀬 安希, 本橋 ほづみ, 菅澤 薫
    第74回日本癌学会学術総会, Oct. 2015, Japanese, 日本癌学会, 名古屋, Domestic conference
    Poster presentation

  • ユビキチンープロテアソーム系による紫外線誘発DNA損傷応答制御
    酒井 恒, 金子雄貴, 岸本藍子, 松井豪志, 赤木純一, Sugasawa Kaoru
    第23回DNA複製・組換え・修復ワークショップ, Oct. 2015, Japanese, 焼津, Domestic conference
    Oral presentation

  • ユビキチンープロテアソーム系による紫外線誘発DNA損傷応答制御
    酒井 恒, 金子 雄貴, 岸本 藍子, 松井 豪志, 赤木 純一, 菅澤 薫
    第23回DNA複製・組換え・修復ワークショップ, Oct. 2015, Japanese, DNA複製・組換え・修復ワークショップ研究会, 焼津, Domestic conference
    Oral presentation

  • 紫外線損傷修復におけるXPCタンパク質の脱ユビキチン化制御機構の解析
    酒井 恒, 岸本藍子, 松井豪志, 赤木純一, Sugasawa Kaoru
    日本遺伝学会第87回大会, Sep. 2015, Japanese, 日本遺伝学会, 仙台, Domestic conference
    Oral presentation

  • 紫外線損傷修復におけるXPCタンパク質の脱ユビキチン化制御機構の解析
    酒井 恒, 岸本 藍子, 松井 豪志, 赤木 純一, 菅澤 薫
    日本遺伝学会第87回大会, Sep. 2015, Japanese, 日本遺伝学会, 仙台, Domestic conference
    Oral presentation

  • Molecular mechanism of DNA damage recognition in mammalian nucleotide excision repair.
    Onishi Y, Tone D, Kinoshita M, Iwai S, Sakai W, Sugasawa Kaoru
    15th International Congress of Radiation Research, May 2015, English, 京都, International conference
    Oral presentation

  • Molecular mechanism of DNA damage recognition in mammalian nucleotide excision repair.
    Onishi Y, Tone D, Kinoshita M, Iwai S, Sakai W, Sugasawa, K
    15th International Congress of Radiation Research, May 2015, English, ICRR, 京都, International conference
    Oral presentation

  • ヌクレオチド除去修復の制御に関わるクロマチン構造動態
    中西 正哉, 各務 恵理菜, 酒井 恒, SUGASAWA KAORU
    日本薬学会第135年会, Mar. 2015, Japanese, 神戸学院大学, Domestic conference
    Oral presentation

  • In Vivo Regulation of Mammalian Nucleotide Excision Repair
    Sugasawa, K
    The Mammalian DNA Repair Gordon Research Conference 2015, Feb. 2015, English, Four Points Sheraton / Holiday Inn Express, International conference
    [Invited]
    Invited oral presentation

  • 哺乳類ヌクレオチド除去修復タンパク質XPCのDNA結合モードの1分子イメージング
    横田 浩章, 戸根 大輔, 大西 優貴, 韓 龍雲, 原田 慶恵, 菅澤 薫
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Oral presentation

  • 翻訳後修飾を介した色素性乾皮症遺伝子産物の機能制御
    秋田 眞季, 松本 翔太, 井倉 毅, 酒井 恒, SUGASAWA KAORU
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Oral presentation

  • 遺伝性疾患の分子病態：分子機能から高次生命機能へ
    高田 穣, 菅澤 薫
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Oral presentation

  • ヒトRAD52タンパク質のアセチル化制御
    安田 武嗣, 香川 亘, 齋藤 健吾, 荻 朋男, 花岡 文雄, 菅澤 薫, 胡桃坂 仁志, 田嶋 克史
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復におけるDNA損傷認識機構の解析
    大西 優貴, 戸根 大輔, 木下 実, 岩井 成憲, 菅澤 薫
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Poster presentation

  • ヌクレオソームにおける紫外線損傷塩基の収納およびその認識機構の解析
    越阪部 晃永, 立和名 博昭, 堀越 直樹, 香川 亘, 山元 淳平, 安田 武嗣, 花岡 文雄, SUGASAWA KAORU, 岩井 成憲, 胡桃坂 仁志
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Poster presentation

  • ゲノム損傷応答におけるGadd45αの機能解析
    小山 紗季, 北野 健太, INASE AKI, 酒井 恒, 菅澤 薫
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Poster presentation

  • SUMO regulates DNA damage recognition in nucleotide excision repair
    Akita, M, Tak, Y.-S, Shimura, T, Matsumoto, S, Ikura, T, Sugasawa, K
    The 9th 3R Symposium Together with National Instituite of Genetics 2014 International Symposium, Nov. 2014, English, 御殿場高原ホテル, International conference
    Poster presentation

  • Studies on the de-ubiquitination mechanism of the xeroderma pigmentosum group C protein
    Kishimoto, A, Akagi, J, Matsui, T, Matsumoto, S, Sakai, W, Sugasawa, K
    The 9th 3R Symposium Together with National Instituite of Genetics 2014 International Symposium, Nov. 2014, English, 御殿場高原ホテル, International conference
    Poster presentation

  • Post-translational modifications coordinating recognition and repair of UV-induced DNA damage
    Sugasawa, Kaoru
    Symposium Together with National Instituite of Genetics 2014 International Symposium, Nov. 2014, English, 御殿場高原ホテル, International conference
    Oral presentation

  • Functional regulation of thymine DNA glycosylase involved in DNA repair and epigenetic reprogramming
    Nakamura, T, Murakami, K, Uehara, Y, Ono, T, Urano, T, Nishitani, H, Sugasawa, K
    The 9th 3R Symposium Together with National Instituite of Genetics 2014, Nov. 2014, English, 御殿場高原ホテル, International conference
    Poster presentation

  • Functional interactions between XPC and DDB2 in nucleotide excision repair
    Shota Matsumoto, Eric S. Fischer, Nicolas H. Thomä, Kaoru Sugasawa
    The 9th 3R Symposium 2014, Nov. 2014, English, 3R organizing committee, 御殿場, International conference
    Poster presentation

  • DNA損傷応答におけるDDB2の翻訳後修飾の機能解析
    松本 翔太, Fischer, E. S, Thomä, N. H, 酒井 恒, 菅澤 薫
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Poster presentation

  • DNA修復・損傷応答におけるクロマチン構造ダイナミクスの解析
    各務 恵理菜, 中西 正哉, 酒井 恒, 木村 宏, 菅澤 薫
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Poster presentation

  • DNA修復とエピゲノム制御に関わるチミンDNAグリコシラーゼの機能制御
    中村 知史, 村上 浩一, 上原 芳彦, 小野 哲也, 浦野 健, 西谷 秀男, 菅澤 薫
    第37回日本分子生物学会年会, Nov. 2014, Japanese, パシフィコ横浜, Domestic conference
    Poster presentation

  • 紫外線誘発DNA損傷修復の細胞内制御機構
    SUGASAWA KAORU
    日本放射線影響学会第57回大会, Oct. 2014, Japanese, かごしま県民交流センター, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復におけるXPCとDDB2の機能的相互作用
    松本 翔太, Fischer Eric S, Thoma Nicolas H, 菅澤 薫
    第87回日本生化学会大会, Oct. 2014, Japanese, 国立京都国際会館, Domestic conference
    Oral presentation

  • Post-translational modifications coordinating recognition and repair of UV-induced DNA damage.
    Sugasawa, Kaoru
    第5回日米修復会議, Oct. 2014, English, グランドエクシブ鳴門, International conference
    Oral presentation

  • 紫外線損傷修復におけるXPCタンパク質の脱ユビキチン化機構の解析
    岸本 藍子, 赤木 純一, 松井 豪志, 酒井 恒, 菅澤 薫
    日本遺伝学会第86回大会, Sep. 2014, Japanese, 長浜バイオ大学, Domestic conference
    Poster presentation

  • Genotype -Phenotype Correlation Among Xeroderma Pigmentosum Complementation Group D.
    Nakano Eiji, Ono Ryusuke, Masaki Taro, Seiji Takeuchi, Takaoka Yutaka, Sugasawa Kaoru, Nishigori Chikako
    3rd Eastern Asia Dermatology Congress, Sep. 2014, English, Eastern Asia Dermatology Congress, Jeju, Korea, 韓国, International conference
    Public symposium

  • 細胞の紫外線損傷DNA修復能の蛍光検出
    栂 達也, 倉岡 功, 渡邉 駿, Nakano Eiji, 竹内 聖二, Nishigori Chikako, Sugasawa Kaoru, 岩井 成憲
    第36回日本光医学・光生物学会, Jul. 2014, Japanese, 日本光医学・光生物学会, 大阪, Domestic conference
    Oral presentation

  • SUMO regulates DNA damage recognition in nucleotide excision repair
    Akita, M, Tak, Y.-S, Shimura, T, Matsumoto, S, Sugasawa,K
    International Symposium on Xeroderma Pigmentosum and Related Diseases, Mar. 2014, English, Kobe, Japan, International conference
    Poster presentation

  • Roles for post-translational protein modifications in regulation of DNA damage recognition for mammalian nucleotide excision repair
    Akita, M, Matsumoto, S, Sakai,W, Sugasawa,K
    International Symposium on Xeroderma Pigmentosum and Related Diseases, Mar. 2014, English, Kobe, Japan, International conference
    Oral presentation

  • Molecular analysis of DNA repair defects in cells from Japanese patients with xeroderma pigmentosum Group D
    Mayca Pozo, F, Sakai,W, van der Spek, P. J, Nakazawa, Y, Ogi, T, Ono, R, Nishigori, C, Sugasawa,K
    International Symposium on Xeroderma Pigmentosum and Related Diseases, Mar. 2014, English, Kobe, Japan, International conference
    Poster presentation

  • Functional interactions between XPC and DDB2 through ubiquitylation in DNA damage responses
    Matsumoto, S, Fischer, E. S, Thomä, N. H, Sugasawa,K
    International Symposium on Xeroderma Pigmentosum and Related Diseases, Mar. 2014, English, Kobe, Japan, International conference
    Poster presentation

  • A child case of xeroderma pigmentosum group D.
    R Ono, T Masaki, E Nakano, FM Pozo, Sakai Wataru, PJ van der Spek, S Takeuchi, T Ogi, Sugasawa Kaoru, C Nishigori
    International Symposium on Xeroderma Pigmentosum and related diseases, Mar. 2014, English, Kobe, International conference
    Poster presentation

  • 哺乳類ヌクレオチド除去修復におけるDNA損傷認識課程の制御
    菅澤 薫
    第36回日本分子生物学会年会, Dec. 2013, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Oral presentation

  • 哺乳類ヌクレオチド除去修復タンパク質XPCの１分子イメージング：DNA上での１次元自由拡散運動の観察
    横田 浩章, 戸根 大輔, 韓 龍雲, 原田 慶恵, 菅澤 薫
    第36回日本分子生物学会年会, Dec. 2013, Japanese, 神戸, Domestic conference
    Poster presentation

  • 酸化的脱メチル化酵素ALKBH2/3の発現変化が細胞増殖・代謝に及ぼす影響
    稲瀬 安希, Irino Yasuhiro, 加香 孝一郎, 小島 真梨子, 深水 昭吉, Sugasawa Kaoru
    第36回日本分子生物学会年会, Dec. 2013, Japanese, 日本分子生物学会, 神戸, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復の損傷認識に関わるクロマチン構造制御
    中西 正哉, 酒井 恒, 白鳥 広海, 木村 宏, 菅澤 薫
    第36回日本分子生物学会年会, Dec. 2013, Japanese, 神戸, Domestic conference
    Poster presentation

  • FANCD2タンパク質はアポトーシスを抑制的に制御する
    SAKAI WATARU, SUGASAWA KAORU
    第36回日本分子生物学会年会, Dec. 2013, Japanese, 神戸, Domestic conference
    Oral presentation

  • DNA脱メチル化酵素TDGのSUMO化修飾による機能制御
    森山 大志, 浦野 健, 菅澤 薫, 斉藤 寿仁
    第36回日本分子生物学会年会, Dec. 2013, Japanese, 神戸, Domestic conference
    Poster presentation

  • DNA損傷応答におけるXPCとDDB2のユビキチン化を介した機能連関
    松本 翔太, Fischer, E. S, Thomä, N. H, 菅澤 薫
    第36回日本分子生物学会年会, Dec. 2013, Japanese, 神戸, Domestic conference
    Poster presentation

  • DNA修復異常を伴う光線過敏症患者の分子細胞生物学的解析
    酒井 恒, Franklin Mayca Pozo, 菅澤 薫, 中沢 由華, 荻 朋男, 小野 竜輔, 錦織 千佳子
    厚生労働省科学研究費「神経皮膚症候群に関する調査研究班」平成25年度総会, Dec. 2013, Japanese, 神経皮膚症候群に関する調査研究班, 東京, Domestic conference
    Others

  • DNA修復とエピゲノム制御に関わるチミンDNAグリコシラーゼの機能制御
    中村 知史, 村上 浩一, 上原 芳彦, 小野 哲也, 浦野 健, 西谷 秀男, 菅澤 薫
    第36回日本分子生物学会年会, Dec. 2013, Japanese, 神戸, Domestic conference
    Poster presentation

  • ファンコニ貧血症タンパク質FANCD2によるアポトーシス制御機構
    SAKAI WATARU, SUGASAWA KAORU
    第31回染色体ワークショップ・第12回核ダイナミクス研究会, Nov. 2013, Japanese, 箱根, Domestic conference
    Oral presentation

  • ファンコニ貧血症タンパク質FANCD2によるアポトーシス制御機構
    SAKAI WATARU, SUGASAWA KAORU
    第22回DNA複製・組換え・修復ワークショップ, Nov. 2013, Japanese, 仙台, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復における損傷認識機構とSUMO化修飾の意義
    AKITA masaki, MATSUMOTO syota, SUGASAWA kaoru
    第22回 DNA 複製・組換え・修復ワークショップ, Nov. 2013, Japanese, Domestic conference
    Oral presentation

  • Manipulated expression of the oxidative DNA/RNA demethylation enzymes ALKBH2/3 alters cellular proliferation and metabolism.
    Inase, A, Irino, Y, Kako, K, Kojima, M, Fukamizu, A, Sugasawa,K
    International Symposium on Transcription and Metabolism, Nov. 2013, English, Awaji, Japan, International conference
    Oral presentation

  • Functional regulation of thymine DNA glycosylase involved in DNA repair and epigenetic reprogramming
    Nakamura, T, Murakami, K, Uehara, Y, Ono, T, Urano, T, Nishitani, T, Sugasawa,K
    International Symposium on Transcription and Metabolism, Nov. 2013, English, Awaji, Japan, International conference
    Oral presentation

  • Functional interactions of DNA damage repair with transcriptional and epigenetic regulation
    Matsumoto, S, Nakanishi, S, Sakai,W, Sugasawa,K
    International Symposium on Transcription and Metabolism, Nov. 2013, English, Awaji, Japan, International conference
    Oral presentation

  • DNA損傷応答におけるXPCとDDB2のユビキチン化を介した機能連関
    松本 翔太, Fischer, E. S, Thomä, N. H, 菅澤 薫
    第22回DNA複製・組換え・修復ワークショップ, Nov. 2013, Japanese, 仙台, Domestic conference
    Oral presentation

  • Chromatin structure regulating DNA damage recognition in nucleotide excision repair
    Nakanishi, S, Sakai,W, Shiratori, H, Kimura, H, Sugasawa,K
    International Symposium on Transcription and Metabolism, Nov. 2013, English, Awaji, Japan, International conference
    Oral presentation

  • 哺乳類ヌクレオチド除去修復タンパク質XPCの1分子イメージング
    横田 浩章, 西幹 栄美, 戸根 大輔, 韓 龍雲, 原田 慶恵, 菅澤 薫
    第51回日本生物物理学会年会, Oct. 2013, Japanese, 京都, Domestic conference
    Poster presentation

  • 紫外線誘発DNA損傷の修復機構におけるSUMO化修飾の役割
    AKITA MASAKI, SAKAI WATARU, SUGASAWA KAORU
    日本放射線影響学会第56回大会, Oct. 2013, Japanese, 青森, Domestic conference
    Oral presentation

  • 酸化的脱メチル化酵素ALKBH2/3の発現変化が細胞増殖・代謝に及ぼす影響
    稲瀬 安希, 入野 康宏, 加香 孝一郎, 小島 真梨子, 深水 昭吉, 菅澤 薫
    第36回日本分子生物学会年会, Oct. 2013, Japanese, 神戸, Domestic conference
    Poster presentation

  • メチル化塩基修飾酵素ALKBH2/3の発現変化が代謝に与える影響
    稲瀬 安希, 入野 康宏, 加香 孝一郎, 小島 真梨子, 深水 昭吉, 菅澤 薫
    第1回がんと代謝研究会, Oct. 2013, Japanese, 鶴岡, Domestic conference
    Poster presentation

  • ゲノムDNA損傷の修復と細胞応答を制御するタンパク質翻訳後修飾の役割
    菅澤 薫
    第86回日本生化学会大会, Sep. 2013, Japanese, 横浜, Domestic conference
    Oral presentation

  • FANCD2はDNA修復に関わる機能とは独立してTNFα/TNFR1を介したアポトーシス機構を負に制御している
    SAKAI WATARU, SUGASAWA KAORU
    第22回日本Cell Death学会学術集会, Jul. 2013, Japanese, 京都, Domestic conference
    Oral presentation

  • Regulation of the DNA damage recognition machinery in mammalian nucleotide excision repair
    SUGASAWA KAORU
    第36回日本分子生物学会年会, 2013, English, 神戸, Domestic conference
    Oral presentation

  • FANCD2遺伝子産物はDNA修復とは独立したアポトーシス抑制機能を有する
    SAKAI WATARU, SUGASAWA KAORU
    日本遺伝学会第85回大会, 2013, Japanese, 横浜, Domestic conference
    Oral presentation

  • The Functional Analysis of the Modifications of the DNA Damage Recognition Protein DDB2(2W5II-6)
    Matsumoto, S, Fischer, E. S, Yoshino, K, Thomä, N. H, Sugasawa,K
    第35回日本分子生物学会年会, Dec. 2012, Japanese, 福岡, Domestic conference
    Keynote oral presentation

  • Roles of sumoylation in regulation of the xeroderma pigmantosum group C protein
    AKITA masaki, TAK Yon-Soo, SHIMURA tsutomu, HANAOKA fumio, SUGASAWA kaoru
    第35回 日本分子生物学会年会 ポスター発表, Dec. 2012, Japanese, Domestic conference
    Oral presentation

  • Novel function of RFC complexes in genome stability through PCNA-CRL4Cdt2 mediated (3W5III-5) Cdt1Degradation During DNA Replication.
    Shiomi,Y, Hayashi,A, Ishii,T, Nakayama,J, Sugasawa,K, Nishitani,H
    第35回日本分子生物学会年会, Dec. 2012, Japanese, 福岡, Domestic conference
    Keynote oral presentation

  • FANCD2 タンパク質はアポトーシスを抑制的に制御する
    酒井 恒, 菅澤 薫
    第30回染色体ワークショップ, Dec. 2012, Japanese, 淡路, Domestic conference
    Public symposium

  • Exploration of Novel Regulatory Factors in Mammalian Nucleotide Excision Repair (1ST3-018)
    Tone,D, Yoshino,K, Iwai,S, Sugasawa,K
    第35回日本分子生物学会年会, Dec. 2012, Japanese, 福岡, Domestic conference
    Poster presentation

  • Elucidation of a Linkage Between Ubiquitin E3 Ligase RNF4 and a Component of the (1ST3-022) Thymine DNA Glycosylase TDG-containing DNA Demethylation Complex.
    Yoshikai,Y, Moriyama, T, Fujimitsu,Y, Sasano,T, Tateishi,S, Sugasawa,K, Urano,T, Iwai,K, Saitoh,H
    第85回日本生化学会, Dec. 2012, Japanese, 福岡, Domestic conference
    Poster presentation

  • DNA damage induced-acetylation of human Rad52 protein is required for appropriate accumulation of the protein at DNA double-strand break sites.
    Yasuda, T, Saito, K, Kagawa, W, Ogi, T, Suzuki, T, Dohmae, N, Hino, T, Nakazawa, Y, Ai Saotome-Nakamura, Kato, T, Genet, M, Hazawa, M, Tomita, M, Hanaoka, F, Sugasawa, K, Jeggo,P, Okayasu, R, Tajima, K, Kurumizaka,H
    第35回日本分子生物学会年会, Dec. 2012, Japanese, 日本分子生物学会, 福岡, Domestic conference
    Keynote oral presentation

  • DNA damage-induced acetylation of human Rad52 protein in human mesenchymal stem cells
    Saotome-Nakamura A, Yasuda Takahiro, Saito K, Kagawa W, Ogi T, Suzuki T, Dohmae N, Hino T, Nakazawa Y, Hazawa M, Hanaoka F, Sugasawa Kaoru, Okayasu R, Kurumizaka H, Tajima K
    第35回日本分子生物学会年会, Dec. 2012, Japanese, 日本分子生物学会, 福岡, Domestic conference
    Poster presentation

  • A novel function of FANCD2 protein in apoptosis signaling (2ST2-026)
    Sakai, W, Sugasawa,K
    第35回日本分子生物学会年会, Dec. 2012, Japanese, 日本分子生物学会, 福岡, Domestic conference
    Poster presentation

  • A novel function of centrin-2 involved in maintenance of genomic stability.
    SUGASAWA KAORU, Nishi,R, SAKAI WATARU, TONE DAISUKE, Hanaoka,F
    第35回日本分子生物学会, Dec. 2012, Japanese, 福岡, Domestic conference
    Oral presentation

  • A novel function of centrin-2 involved in maintenance of genomic stability
    Sugasawa Kaoru, Nishi R, Sakai W, Tone D, Hanaoka F
    第35回日本分子生物学会年会, Dec. 2012, Japanese, 日本分子生物学会, 福岡, Domestic conference
    Keynote oral presentation

  • SUMO regulates DNA damage recognition in nucleotide excision repair.
    Akita,M, Tak,Yon-Soo, Shimura, T, Matsumoto, S, Sugasawa,K
    The 8th 3R Symposium (International Symposium on DNA Replication, Recombination and Repair), Nov. 2012, English, Awaji, International conference
    Public symposium

  • Genotoxic stress induces caspase-mediated cleavage of the FANCD2 protein.
    Sakai,W, Sugasawa,K
    The 8th 3R Symposium (International Symposium on DNA Replication, Recombination and Repair), Nov. 2012, English, Awaji, International conference
    Public symposium

  • Functional studies on ubiquitylation of the DNA damage recognition protein DDB2
    Matsumoto,S, Fischer, E. S, Yoshino,K, Thomä, N. H, Sugasawa,K
    The 8th 3R Symposium (International Symposium on DNA Replication, Recombination and Repair), Nov. 2012, English, Awaji, International conference
    Public symposium

  • DNA損傷応答とSUMO／ubiquitin
    秋田眞季, Sugasawa Kaoru
    第10回SUMO 研究会, Nov. 2012, Japanese, SUMO 研究会, 熊本, Domestic conference
    Oral presentation

  • DNA repair synthesis defect in xeroderma pigmentosum group D cells.
    Mayca Pozo, F, Sakai, W, Peter J. van, der Spek, Nakazawa,Y, Ogi, T, Nishigori,C, Sugasawa,K
    The 8th 3R Symposium (International Symposium on DNA Replication, Recombination and Repair), Nov. 2012, English, Awaji, International conference
    Public symposium

  • 紫外線損傷修復におけるXPCタンパク質の脱ユビキチン化機構の解析
    赤木 純一, 松井 豪志, SAKAI WATARU, SUGASAWA KAORU
    日本遺伝学会第84回大会, Sep. 2012, Japanese, 福岡, Domestic conference
    Oral presentation

  • 紫外線によるDNA損傷の修復を促進するDDB2の構造と機能制御
    MATSUMOTO SHOTA, 安田 武嗣, Eric S. Fischer, Nicolas H. Thomä, 花岡 文雄, SUGASAWA KAORU
    日本放射線影響学会第55回大会, Sep. 2012, Japanese, 仙台, Domestic conference
    Oral presentation

  • Functional regulation of the DNA damage recognition factor DDB2 via post-translational modifications.
    Sugasawa,K, Hanaoka, F
    第71回日本癌学会学術総会, Sep. 2012, Japanese, 札幌, Domestic conference
    Oral presentation

  • 紫外線誘発DNA損傷の認識と修復の分子基盤
    菅澤 薫
    第34回日本光医学・光生物学会, Jul. 2012, Japanese, 神戸大学大学院医学研究科, 神戸, Domestic conference
    [Invited]
    Invited oral presentation

  • Post-Translational Protein Modification Regulating Mammalian Nucleotide Excision Repair.
    Sugasawa,K
    US-JAPAN DNA Repair Meeting, Apr. 2012, English, Virginia, USA, International conference
    [Invited]
    Invited oral presentation

  • Molecular mechanism of DNA damage recognition in mammalian nucleotide excision repair.
    Sugasawa,K
    DNA Repair Mini-Symposium, Apr. 2012, English, Maryland, USA, International conference
    [Invited]
    Invited oral presentation

  • タンパク質翻訳後修飾によるDNA損傷認識の制御
    SUGASAWA Kaoru
    国立遺伝学研究所研究集会「ユビキチン・SUMOによるDNA複製およびDNA修復系の制御」, Feb. 2012, Japanese, 国立遺伝学研究所, 三島, Domestic conference
    Oral presentation

  • DNA損傷ストレスに伴うFANCD2タンパク質のカスパーゼ依存的切断
    酒井 恒, 菅澤 薫
    第29回染色体ワークショップ, Jan. 2012, Japanese, 仙台, Domestic conference
    Oral presentation

  • Roles for sumoylation in regulation of the xeroderma pigmentosum group C protein
    秋田眞季, Sugasawa Kaoru
    Kobe University-University of Washington Joint Symposium on Integrative Membrane Biology and Signal Transduction Medeicine, Dec. 2011, English, 神戸, International conference
    Poster presentation

  • Roles for sumoylation in regulation of the xeroderma pigmentosum group C protein
    Masaki Akita, Yon-Soo Tak, Tsutomu Shimura, Fumio Hanaoka, Kaoru Sugasawa
    第34回日本分子生物学会年会, Dec. 2011, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Oral presentation

  • Regulation of active DNA demethylation enzyme, the thymine DNA glycosylase TDG, by SUMOylation and ubiquitinylation
    Taishi Moriyama, Yuka Fujimitsu, Yushi Yoshikai, Takeshi Urano, Kaoru Sugasawa, Tetsuya Ono, Kazuhumi Takamune, Hisato Saito
    第34回日本分子生物学会年会, Dec. 2011, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Oral presentation

  • Reconstitution of mammalian nucleotide excision repair:molecular basis for DNA damage recognition
    Kaoru Sugasawa, Daisuke Tone, Takeshi Yasuda, Fumio Hanaoka
    第34回日本分子生物学会年会, Dec. 2011, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Oral presentation

  • New function of PCNA loaders, RFC1-RFC and Ctf18-RFC, in genome stability through PCNA-CRL4-mediated Cdt1 degradation
    Yasushi Shiomi, Akiyo Hayashi, Naohiro Suenaga, Miyuki Tanaka, Jun-ichi Nakayama, Kaoru Sugasawa, Hideo Nishitani
    第34回日本分子生物学会年会, Dec. 2011, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Oral presentation

  • Genotoxic stress induces caspase-mediated cleavage of the FANCD2 protein
    Wataru Sakai, Kaoru Sugasawa
    第34回日本分子生物学会年会, Dec. 2011, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Oral presentation

  • Functional analysis of the CRL4 DDB2 E3 ligase in mammalian nucleotide excision repair
    Syota Matsumoto, Takeshi Yasuda, Naoshi Dohmae, Eric S.Fischer, Nicolas H.Thoma, Ryotaro Nishi, Fumio Hanaoka, Kaoru Sugasawa
    第34回日本分子生物学会年会, Dec. 2011, Japanese, 日本分子生物学会, 横浜, Domestic conference
    Oral presentation

  • DNA damage recognition in nucleotide excision repair: molecular mechanism and involvement of chromatin structure.
    Kaoru Sugasawa
    The 27th RBC-NIRS International Symposium on "Chromatin Dynamics and Epigenetic Memory in DNA Damage Response", Dec. 2011, English, Kyoto University, コープイン京都, International conference
    [Invited]
    Invited oral presentation

  • ヌクレオチド除去修復におけるDNA損傷認識の分子基盤
    菅澤 薫
    日本放射線影響学会第54回大会, Nov. 2011, Japanese, 日本放射線影響学会, 神戸, Domestic conference
    [Invited]
    Invited oral presentation

  • Regulationn of DNA repair through post-translational protein modifications.
    Kaoru Sugasawa
    Taiwan-Japan Joint Symposium on Cell Signaling and Gene Regulation, Nov. 2011, English, National Cheng Kung University, Tainan, Taiwan, International conference
    [Invited]
    Invited oral presentation

  • DNA損傷修復とエピゲノム制御のクロストーク
    Kaoru Sugasawa
    第12回Wakoつくばフォーラム, Nov. 2011, Japanese, 和光純薬工業, 筑波和光ホール, Domestic conference
    [Invited]
    Invited oral presentation

  • ヌクレオチド除去修復の損傷認識機構におけるSUMO化修飾の役割
    AKITA masaki, SUGASAWA Kaoru
    第10回核ダイナミクス研究会, Oct. 2011, Japanese, 核ダイナミクス研究会, 北海道 北広島, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復におけるDNA損傷認識機構とUV-DDBの役割
    Kaoru Sugasawa
    平成23年度遺伝研研究会｢クロマチンダイナミクスの分子機構」, Oct. 2011, Japanese, 国立遺伝学研究所, 三島, Domestic conference
    [Invited]
    Invited oral presentation

  • SUMO認識型ユビキチンリガーゼRNF4によるTDGグリコシラーゼを含むDNA脱メチル化酵素複合体の機能制御
    Y. Yoshikai, Y. Fujimitsu, T. Sasano, S. Tateishi, K. Sugasawa, T. Urano, K. Iwai, H. Saito
    第84回日本生化学会大会, Sep. 2011, Japanese, 日本生化学会, 国立京都国際会館, Domestic conference
    Oral presentation

  • UV-DDB:ヌクレオチド除去修復とエピゲノム制御のクロスロード
    Kaoru Sugasawa
    構造エピゲノム研究会第４回ワークショップ「DNA損傷とエピゲノム」, Jul. 2011, Japanese, 構造エピゲノム研究会, 理化学研究所横浜研究所交流棟ホール, Domestic conference
    [Invited]
    Invited oral presentation

  • Regulation of DNA damage recognition in mammalian NER
    Kaoru Sugasawa
    Conference on Responses to DNA Damage: from Molecular Mechanism to Human Disease, Apr. 2011, English, Organizing Committee, Conference on Responses to DNA damage, Egmond aan Zee, The Netherlands, International conference
    [Invited]
    Invited oral presentation

  • 複製と損傷に応答して機能するユビキチンリガーゼ、CRL4Cdt2の制御機構
    Yasushi Shiomi, Ryotaro Nishi, Kaoru Sugasawa, Junichi Nakayama
    第33回日本分子生物学会年会, Dec. 2010, Japanese, 日本分子生物学会, 神戸ポートアイランド, Domestic conference
    Oral presentation

  • Functional analysis of the N-terminal domain of the DNA damage recognition protein DDB2
    Syota Matsumoto, Takeshi Yasuda, Naoshi Dohmae, Kouichi Murakami, Ryotaro Nishi, Fumio Hanaoka, Kaoru Sugasawa
    第33回日本分子生物学会年会・第83回日本生化学会大会合同大会, Dec. 2010, Japanese, 日本分子生物学会, 神戸ポートアイランド, Domestic conference
    Oral presentation

  • DNA損傷ストレスに伴うFANCD2タンパク質のカスパーゼ依存的切断
    Wataru Sakai, Kaoru Sugasawa
    第33回日本分子生物学会年会・第83回日本生化学会大会合同大会, Dec. 2010, Japanese, 日本分子生物学会, 神戸ポートアイランド, Domestic conference
    Oral presentation

  • A 19S proteasome subunit PSMD14 is involved in deubiquitination of XPC
    Junichi Akagi, Fumio Hanaoka, Kaoru Sugasawa
    第33回日本分子生物学会年会・第83回日本生化学会大会合同大会, Dec. 2010, Japanese, 日本分子生物学会, 神戸ポートアイランド, Domestic conference
    Poster presentation

  • Roles for centrin-2 in DNA damage recognition for global genome nucleotide excision repair
    Kaoru Sugasawa, Ryotaro Nishi, Yon-Soo Tak, Wataru Sakai, Fumio Hanaoka
    The 7th 3R Symposium (International Symposium on DNA Replication, Recombination and Repair), Oct. 2010, English, 第7回3Rシンポジウム実行委員会, 富山国際会議場, Domestic conference
    Oral presentation

  • Genotoxic stress induces caspase-mediated cleavage of the FANCD2 protein
    Kaoru Sugasawa, Wataru Sakai
    The 7th 3R Symposium (International Symposium on DNA Replication, Recombination and Repair), Oct. 2010, English, 第7回3Rシンポジウム実行委員会, 富山, Domestic conference
    Poster presentation

  • Molecular basis for DNA damage recognition by xeroderma pigmentosum gene products
    Kaoru Sugasawa, Fumio Hanaoka
    第69回日本癌学会学術総会, Sep. 2010, Japanese, 日本癌学会, 大阪, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復におけるcentrin2の機能解析
    菅澤 薫
    国立遺伝学研究所研究集会「ユビキチン・SUMOによるDNA複製およびDNA修復系の制御」, Sep. 2010, Japanese, 国立遺伝学研究所, 三島, Domestic conference
    Oral presentation

  • ゲノム全体を監視するDNA損傷認識の分子基盤
    Sugasawa Kaoru, 安田 武嗣, 赤木 純一, 西 良太郎, 岩井 成憲, 花岡 文雄
    第9回核ダイナミクス研究会, May 2010, Japanese, 核ダイナミクス研究会, 伊豆, Domestic conference
    Oral presentation

  • DNA damage recognition mechanism for mammalian nucleotide excision repair
    Sugasawa Kaoru
    International Conference on Radiation and Cancer Biology at Nagasaki 2010, Feb. 2010, English, Nagasaki University, Nagasaki, Japan, International conference
    Invited oral presentation

  • Post-translational modification of XPC protein controls global genome nucleotide excision repair
    Tak, Y.-S, Shimura, T, Ryotaro Nishi, Okuda-Shimizu, Y, Shimizu, Y, Hanaoka, F, Sugasawa Kaoru
    第32回日本分子生物学会年会, Dec. 2009, English, 日本分子生物学会, パシフィコ横浜, Domestic conference
    Poster presentation

  • Genotoxic stress targets Fanconi anemia group D2 protein for fragmentation by the caspase-mediated pathway
    Sakai Wataru, Sugasawa Kaoru
    第32回日本分子生物学会年会, Dec. 2009, Japanese, 日本分子生物学会, パシフィコ横浜, Domestic conference
    Poster presentation

  • Fluorescence detection of cellular ability of base excision repair
    栂 達也, 松本 直之, Kaoru Sugasawa, 倉岡 功, 岩井 成憲
    第32回日本分子生物学会年会, Dec. 2009, Japanese, 日本分子生物学会, パシフィコ横浜, Domestic conference
    Poster presentation

  • DNA damage recognition coordinated by the multiple xeroderma pigmentosum gene products
    Sugasawa Kaoru
    第32回日本分子生物学会年会, Dec. 2009, Japanese, 日本分子生物学会, パシフィコ横浜, Domestic conference
    Oral presentation

  • Centrin 2 mediates interaction between XPC and DDB2
    Nishi Ryotaro, Wim Vermeulen, Jan H.J. Hoejimakers, Hanaoka Fumio, Sugasawa Kaoru
    第32回日本分子生物学会年会, Dec. 2009, Japanese, 日本分子生物学会, パシフィコ横浜, Domestic conference
    Poster presentation

  • Post-translational modifications involved in cellular DNA damage response
    Kaoru Sugasawa
    2009 Japan-Taiwan Joint Symposium on Cell Signaling and Gene Regulation, Nov. 2009, Japanese, Kobe University, National Cheng Kung University, Kobe, International conference
    Oral presentation

  • Centrin 2 は損傷認識因子XPCとDDB2の相互作用を促進する
    Ryotaro Nishi, Vermeulen, W, Hoeijmakers, J. H. J, Iwai S, Hanaoka F, Sugasawa Kaoru
    第20回 DNA複製・組換え・修復ワークショップ, Nov. 2009, Japanese, 3Rワークショップ2009事務局, 琵琶湖コンファレンスセンター, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復に関わるXPCの翻訳後修飾による機能制御
    Sugasawa Kaoru, Yon-Soo Tak
    国立遺伝学研究所研究集会「ユビキチン・SUMOによるDNA複製およびDNA修復系の制御」, Oct. 2009, Japanese, 国立遺伝学研究所, 三島, Domestic conference
    Oral presentation

  • DNA損傷に伴うFANCD2(FA-D2)タンパク質のcaspase依存的切断
    Sakai Wataru, Sugasawa Kaoru
    日本遺伝学会第81回大会, Sep. 2009, Japanese, 日本遺伝学会, 松本, Domestic conference
    Oral presentation

  • Coordinated actions of multiple DNA damage detectors in nucleotide excision repair
    Kaoru Sugasawa
    National Conference on Medical Genomics and Proteomics, Sep. 2009, English, Novosibirsk, Russia, International conference
    [Invited]
    Invited oral presentation

  • Post-translational modification of XPC protein controls global genome nucleotide excision repair
    Tak, Y.-S, Shimura, T, Nishi, R, Okuda-Shimizu, Y, Shimizu, Y, Hanaoka, F, Sugasawa, K
    The 3rd ASM Conference on DNA Repair and Mutagenesis, Jun. 2009, English, American Society for Microbiology, Whistler, BC, Canada, International conference
    Poster presentation

  • Molecular basis for DNA damage recognition in nucleotide excision repair
    Sugasawa Kaoru
    International Symposium on DNA Damage Response and Repair Mechanisms, Apr. 2009, English, The Integrated Project DNA Damage and Response Mechanisms, Crete, Greece, International conference
    Invited oral presentation

  • ヒトリンパ芽球細胞における放射線適応応答
    谷田貝 文雄, Sugasawa Kaoru
    第3回放射線防護研究センターシンポジウム, Dec. 2008, Japanese, 放射線医学総合研究所, 千葉, Domestic conference
    Invited oral presentation

  • ヌクレオチド除去修復におけるゲノム損傷認識機構
    Sugasawa Kaoru
    第3回放射線防護研究センターシンポジウム, Dec. 2008, Japanese, 放射線医学総合研究所, 千葉, Domestic conference
    Invited oral presentation

  • ヌクレオチド除去修復におけるTFIHへリカーゼ活性調節機構の解析
    Akagi Junichi, Sugasawa Kaoru
    BMB2008 第31回日本分子生物学会年会・第81回日本生化学会大会, Dec. 2008, Japanese, 日本分子生物学会・日本生化学会, 神戸, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復におけるDNA損傷認識の分子機序
    Sugasawa Kaoru
    BMB2008 第31回日本分子生物学会年会・第81回日本生化学会大会, Dec. 2008, Japanese, 日本分子生物学会・日本生化学会, 神戸, Domestic conference
    Oral presentation

  • Centrin 2 enhances in vitro nucleotide excision repair via complex formation with xeroderma pigmentosum group C pretein through its C-terminal domain.
    Nishi Ryotaro, Miyake Haruka, Kitano Kenta, Murakami Kouichi, Hanaoka Fumio, Sugasawa Kaoru
    BMB2008 第31回日本分子生物学会年会・第81回日本生化学会大会, Dec. 2008, Japanese, 日本分子生物学会・日本生化学会, 神戸, Domestic conference
    Poster presentation

  • DSB修復効率からの適応応答の追及
    谷田貝 文夫, Sugasawa Kaoru, 榎本 秀, 本間 正充
    日本放射線影響学会第51回大会, Nov. 2008, Japanese, 日本放射線影響学会, 北九州, Domestic conference
    Oral presentation

  • Analysis of mutagenic radioadaptation in human lymphoblastoid cells
    Sugasawa Kaoru, F. Yatagai
    New Nuclear Research Symposium "Biological Response to Low Dose Radiation", Nov. 2008, English, 新原子力基盤クロスオーバー研究「低線量域放射線に特有な生体反応の多面的解析」, Kitakyushu, International conference
    Invited oral presentation

  • Xeroderma pigmentosum proteins and their functions in DNA damage recognition
    Sugasawa Kaoru
    第67回日本癌学会学術総会, Oct. 2008, Japanese, 日本癌学会, 名古屋, Domestic conference
    Oral presentation

  • Molecular mechanisms underlying efficient DNA damage recognition for nucleotide excision repair
    Sugaswa Kaoru, Nishi Ryotaro, Akagi Junichi, Yon-Soo Tak, Kobayashi Hirotaka, Hanaoka Fumio
    The 6th 3R Symposium (International Symposium on DNA Replication, Recombination and Repair), Oct. 2008, English, 第6回3Rシンポジウム実行委員会, Kakegawa, Japan, International conference
    Oral presentation

  • Analyses of regulatory mechanisms of TFIIH helicase activity in nucleotide exicion repair
    Akagi Junichi, Sugasawa Kaoru
    The 6th3R Symposium (International Symposium on DNA Replication, Recombination and Repair), Oct. 2008, English, 第6回3Rシンポジウム実行委員会, Kakegawa, International conference
    Poster presentation

  • Damage recognition mechanism for mammalian nucleotide excision repair
    Sugasawa Kaoru
    Russian-European Workshop on DNA Repair and Epigenetic Regulation of Genome Stability, Jun. 2008, English, Institute of Chemical Biology and Fundermental Medicine, Russia St. Petersburg, International conference
    Oral presentation

  • ヌクレオチド除去修復因子の細胞内動態とその制御機構
    Nishi Ryotaro, Alekseev, S, Dinant, C, Hoogstraten, D, Houtsmuller, A. B, Hoeijmakers, J. H. J, Vermeulen, W, Hanaoka Fumio, Sugasawa Kaoru
    2007年度組換え・染色体再編ワークショップ・第19回DNA複製・分配ワークショップ・合同ワークショップ, Mar. 2008, Japanese, 伊豆, Domestic conference
    Oral presentation

  • 色素性乾皮症C群の小児例
    Sugasawa Kaoru, 小野 竜輔, 正木 太朗, 千代丸 康治, 長野 徹, 錦織 千佳子, 井上 雄二
    第405回（総会）日本皮膚科学会大阪地方会, Feb. 2008, Japanese, 大阪, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復因子の細胞内動態とその制御機構の解析
    Nishi Ryotaro, Alekseev, S, Dinant, C, Hoogstraten, D, Hoeijmakers, J. H. J, Vermeulen, W, Hanaoka Fumio, Sugasawa Kaoru
    シンポジウム「DNA修復研究の最前線」．第30回日本分子生物学会年会・第80回日本生化学会大会 (BMB2007), Dec. 2007, Japanese, 日本分子生物学会・日本生化学会, 横浜, Domestic conference
    Poster presentation

  • ヌクレオチド除去修復における損傷認識とユビキチン化
    Sugasawa Kaoru
    ワークショップ「ユビキチン化を介したゲノムダイナミクスの制御」．第30回日本分子生物学会年会・第80回日本生化学会大会 (BMB2007), Dec. 2007, Japanese, 日本分子生物学会・日本生化学会, 横浜, Domestic conference
    Oral presentation

  • DNA修復因子と転写調節因子のSUMO化による活性調節の構造的基盤
    白川 昌宏, 馬場 大地, 有田 恭平, 立石 幸寬, 斉藤 寿仁, Sugasawa Kaoru, 中井 彰, 関山 直孝, 栃尾 豪人, 有吉 眞理子, 廣明 秀一
    第30回日本分子生物学会年会・第80回日本生化学会大会 (BMB2007), Dec. 2007, Japanese, 日本分子生物学会・日本生化学会, 横浜, Domestic conference
    Oral presentation

  • ヌクレオチド除去修復におけるSUMO化の役割
    Sugasawa Kaoru
    第5回SUMO研究集会, Oct. 2007, Japanese, SUMO研究会, 京都, Domestic conference
    Oral presentation

  • Repair of UV-induced DNA damage: the molecular mechanism preventing skin cancer
    Sugasawa Kaoru, Nishi Ryotaro, Hanaoka Fumiko
    Symposium on "Genomic Instability" in The 66th Annual Meeting of the Japanese Cancer Association., Oct. 2007, English, 日本癌学会, Yokohama, Japan, International conference
    Oral presentation

  • ヌクレオチド除去修復に関わるユビキチン化とSUMO化
    Sugasawa Kaoru
    国立遺伝学研究所研究集会「ユビキチン・SUMOによるDNA複製およびDNA修復系の制御」, Sep. 2007, Japanese, 三島, Domestic conference
    [Invited]
    Invited oral presentation

  • ゲノム損傷修復因子のin vivoダイナミクスとその制御機構
    Nishi Ryotaro, Sugasawa Kaoru
    バイオアーキテクトシンポジウム, Sep. 2007, Japanese, 理化学研究所, 和光, Domestic conference
    Oral presentation

  • Molecular Mechanisms promoting repair of UV-induced DNA damage
    Kaoru Sugasawa
    3rd Japan-US DNA Repair Meeting, May 2007, English, Akira Yasui, Fumio Hanaoka, Kiyoji Tanaka, Errol Friedberg, Samuel Wilson, Hotel Crescent, Akiu, Sendai, International conference
    Invited oral presentation

  • Molecular mechanism of nucleotide excision repair as a defense against cancer
    Kaoru Sugasawa
    International Conference Cellular Responses to DNA Damage and Technical Workshop on DNA Repair, Apr. 2007, English, Institute of Molecular Medicine, National Tsing-Hua University, Hsin-Chu, Taiwan, International conference
    Invited oral presentation

■ Affiliated Academic Society
  • THE JAPANESE ENVIRONMENTAL MUTAGEN SOCIETY

  • THE JAPANESE RADIATION RESEARCH SOCIETY

  • 日本遺伝学会

  • 日本癌学会

  • 日本細胞生物学会

  • 日本薬学会

  • 日本生化学会

  • 日本分子生物学会

■ Research Themes
  • Studies on the principles of chromatin functions ensuring the repair of DNA damage induced by environmental stresses
    菅澤 薫
    Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B), Grant-in-Aid for Scientific Research (B), Kobe University, Apr. 2021 - Mar. 2025, Principal investigator

  • 菅澤 薫
    科学研究費補助金／基盤研究(S), Apr. 2016 - Mar. 2021, Principal investigator
    Competitive research funding

  • 菅澤 薫
    科学研究費補助金／新学術領域研究, Apr. 2016 - Mar. 2018, Principal investigator
    Competitive research funding

  • 色素性乾皮症治療薬の探索
    錦織 千佳子
    国立研究開発法人日本医療研究開発機構,国立大学法人大阪大学, 創薬支援推進事業・創薬総合支援事業, 2017
    Competitive research funding

  • Crosstalk of transcriptional control and energy pathways by hub metabolites
    FUKAMIZU Akiyoshi, IGARASHI Kazuhiko, NAKAO Mitsuyoshi, SUGASAWA Kaoru, MOTOHASHI Hozumi, YAHAGI Naoya, SHIMIZU Toshiyuki, SASAKI Hiroyuki, YONEDA Yoshihiro, KASUGA Masato
    Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area), University of Tsukuba, 01 Apr. 2011 - 31 Mar. 2016
    Our research project aimed to explore the crosstalk between the transcriptional status and energy metabolism. As the organizing group of this project, we held the annual meetings of the research groups and promoted the interaction and collaboration among the members, for example, by setting up “Collaboration Proposal Meeting”. We also supported the workshops organized by graduate students and young scientists, and “Transcription-Metabolism Seminars” held 58 times all over the country. Furthermore, we spread information on a website, held public lectures and announced our achievements to the people through mass media.

  • Single-molecule direct visualization of DNA repair proteins on chromatin
    YOKOTA Hiroaki, SUGASAWA Kaoru, IWAI Shigenori
    Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (C), 01 Apr. 2012 - 31 Mar. 2015
    To elucidate how mammalian (human) DNA repair proteins recognize base lesions, we performed single-molecule direct visualization of the proteins on DNA. We found that XPC-RAD23B protein complex, which is known to be responsible for damage recognition in mammalian nucleotide excision repair, has high affinity for a lesion and performed one-dimensional bidirectional diffusion on undamaged DNA. The diffusion coefficients of the movement indicate that the protein complex does not always perform rotational tracking of the helical pitch of the DNA while moving along DNA and thus diffuses at much higher rates. The obtained results indicate that the protein complex uses these binding modes for efficient search of DNA lesions scattered throughout the genome from a vast excess of normal bases.

  • Detection of structural change of DNA using disulfide bond formation and its application to elucidation of molecular recognition mechanisms
    IWAI Shigenori, SUGASAWA Kaoru, KOJIMA Chojiro
    Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (B), Osaka University, 01 Apr. 2012 - 31 Mar. 2015
    To detect the DNA helix bending by a chemical approach, duplexes containing 2-O-mercaptoalkyl-β-D-arabinofuranose on both sides of the major groove were synthesized, and the effects of the cisplatin adduct, the abasic site analog, and the (6-4) photoproduct on DNA structures were investigated. A disulfide bond was formed depending on the cisplatin adduct, and dynamic DNA bending was shown for the abasic site and the (6-4) photoproduct. Using the bent structure obtained by this method, the model proposed for the handover of damaged DNA from the UV-DDB protein to the XPC protein in the nucleotide excision repair was validated.

  • 菅澤 薫
    科学研究費補助金／基盤研究(A), Apr. 2012 - Mar. 2015, Principal investigator
    Competitive research funding

  • Regulaion of epigenome by the SUMO and ubiquitin modification systems
    SAITOH Hisato, SUGASAWA Kaoru
    Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (C), Kumamoto University, 2011 - 2013
    Thymine DNA glycosylase (TDG) is a base excision repair (BER) enzyme that interacts with the small ubiquitin-related modifier (SUMO)-targeted ubiquitin E3 ligase RNF4 and functions in the active DNA demethylation pathway. Here we found that the majority of TDG was SUMOylated in cells undergoing mitosis, while both SUMOylated and non-modified TDG were eliminated in cells arrested at S phase. In vitro and in vivo binding analyses revealed that TDG interacted with RNF4 in a SUMOylation-independent manner. In RNF4-depleted cells, both forms of TDG were efficiently degraded, suggesting that RNF4 was not the primary E3 ligase for controlling TDG stability. Our findings would not only be important for understanding posttranslational regulation of TDG but also provide implications for the TDG-RNF4 interaction in BER-driven active DNA demethylation during cell cycle progression.

  • 菅澤 薫
    科学研究費補助金／新学術領域研究, 2011, Principal investigator
    Competitive research funding

  • 菅澤 薫
    科学研究費補助金／新学術領域研究, 2011, Principal investigator
    Competitive research funding

  • 厚生科研「神経皮膚症候群に関する調査研究」
    菅澤 薫
    2010, Principal investigator
    Competitive research funding

  • 厚生科研「神経皮膚症候群に関する調査研究」
    菅澤 薫
    2009, Principal investigator
    Competitive research funding

  • ヌクレオチド除去修復におけるＤＮＡ損傷認識初期過程の化学生物学的研究
    菅澤 薫
    2009, Principal investigator
    Competitive research funding

  • 菅澤 薫
    科学研究費補助金／特定領域研究, 2008, Principal investigator
    Competitive research funding

  • 厚生科研「神経皮膚症候群に関する研究」
    菅澤 薫
    2008, Principal investigator
    Competitive research funding

  • 菅澤 薫
    科学研究費補助金／基盤研究(A), 2008, Principal investigator
    Competitive research funding

  • ヌクレオチド除去修復におけるＤＮＡ損傷認識初期過程の化学生物学的研究
    菅澤 薫
    2008, Principal investigator
    Competitive research funding

  • 菅澤 薫
    特別研究員奨励費, 2008, Principal investigator
    Competitive research funding

  • 戦略的：ゲノムの修復機構を基盤とした癌化・老化の制御
    菅澤 薫
    2007, Principal investigator
    Competitive research funding

  • 菅澤 薫
    科学研究費補助金／特定領域研究, 2007, Principal investigator
    Competitive research funding

  • 菅澤 薫
    科学研究費補助金／基盤研究(B), 2007, Principal investigator
    Competitive research funding

  • 厚生科研：神経皮膚症候群に関する研究
    中山 樹一郎
    2007
    Competitive research funding

  • DNA修復機構のネットワークと核構造
    SUGASAWA Kaoru
    2000 - 2004, Principal investigator
    Competitive research funding

  • ヌクレオチド除去修復による遺伝情報維持と細胞機能制御機構
    SUGASAWA Kaoru
    2000 - 2004, Principal investigator
    Competitive research funding

  • Studies on functions of mammalian RAD23 homologs that link DNA repair and protein degradation systems
    SUGASAWA Kaoru
    Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Scientific Research (C), RIKEN (The Institute of Physical and Chemical Reseach), 2000 - 2001
    To examine the possibility of ubiquitylation of the XPC protein that is specifically induced upon DNA damage, FLAG-tagged XPC (FLAG-XPC) and HA-tagged ubiquitin were simultaneously overexpressed in XP4PASV cells, which are derived from a XP group C patient and do not express endogenous XPC protein. By immunoprecipitation of FLAG-XPC from the cell extract, it was demonstrated that XPC can be indeed ubiquitylated in vivo. From similar experiments using various truncated XPC proteins, a domain in XPC was found, which is relatively more susceptible to the ubiquitylation. To investigate possible roles of the XPC ubiquitylation, we established a cell line that stably expresses a physiological amount of FLAG-XPC. When the cells were treated with DNA damaging agents such as UV and 4-NQO, a fraction of XPC became more tightly bound to chromatin, while the majority of ubiquitylated XPC could be solubilized under the same conditions. Moreover, we found that the XPC ubiquitylation occurred in a cell-cycle-independent manner, at least from the Gl/S boundary to the M phase. To explore novel factors that interact with XPC, the yeast two-hybrid screening was carried out, which resulted in the ubiquitin-like protein SUM0-1 as well as the SUMO-1 conjugating enzyme Ubc9.As done for ubiquitylation, we demonstrated that XPC can be also sumoylated in cells by simultaneous overexpression of FLAG-XPC and HA-SUMO-1. Using mouse embryonic fibroblast cells that lack both HR23A and HR23B, we established cell lines that stably express various mutant HR23B proteins. It was shown that the N-terminal ubiquitin-like domain of HR23B is essential neither for intracellular stabilization of XPC nor removal of UV-damage from the global genome.

  • 突然変異に対する防御機構としてのDNA損傷認識機構の解明
    菅澤 薫
    日本学術振興会, 科学研究費助成事業, 特定領域研究(C), 理化学研究所, 2000 - 2000
    哺乳類のゲノム全体で働くヌクレオチド除去修復(NER)副経路において、DNA損傷認識因子として機能するXPC-HR23B複合体のDNAに対する結合特異性の詳細な解析を行なった。特定のDNA損傷や構造を部位特異的に含むDNA断片を用いてゲルシフト法やフットプリント法を行なうことにより、数個の非対合塩基(いわゆるバブル構造)があれば特に損傷が存在しなくてもXPC-HR23Bがこれを認識して結合できることが示された。すなわち、XPC-HR23BはDNA損傷そのものではなく、損傷によって誘起されるDNA構造の歪みを認識して結合すると考えられる。一方、これらのDNA基質を用いて無細胞NER反応を行なったところ、NER機構によるオリゴヌクレオチドの切り出しにはXPC-HR23Bの結合のみでは不十分で、バブル構造中に実際に損傷塩基が存在することが必要であった。以上の結果から、NERにおける損傷認識は(1)XPC-HR23BによるDNAの構造異常の認識、および(2)それに続く損傷塩基の確認、という少なくとも2段階の機構で行われていることが示された。さらに、XPC-HR23Bと相互作用する因子を探索する目的で、XPC蛋白質をbaitとして酵母2ハイブリッド法によるスクリーニングを行ない、複数のポジティブクローンを得た。現在、これらの因子とXPC-HR23Bとの相互作用の意義について、解析を進めている。さらに、XPCや別の損傷結合因子として知られるDDB因子のサブユニットにFLAGタグを融合したものを過剰発現する細胞株の単離を進めており、これを用いて相互作用する因子の解析を今後行なう予定である。

  • ヌクレオチド除去修復機構におけるユビキチン蛋白分解系の役割
    菅澤 薫
    日本学術振興会, 科学研究費助成事業, 特定領域研究(A), 理化学研究所, 1999 - 1999
    RAD23ホモローグと26SプロテアソームのサブユニットS5a蛋白質との相互作用の意義を探る目的で、無細胞蛋白質分解反応系を用いた解析を行った。その結果、ユビキチン-プロテアソームを介した蛋白分解反応に対して、RAD23ホモローグが阻害的に作用することを見いだした。これは、RAD23ホモローグがS5aと結合することによって、ユビキチン化された分解基質蛋白質のプロテアソームとの相互作用を拮抗的に阻害した結果であると考えられた。即ち、RAD23ホモローグはプロテアソームによる蛋白質分解反応に対して、新しいタイプの制御因子として機能する可能性を持つことが示唆された。一方、HR23A、およびHR23Bそれぞれのノックアウトマウスを交配して二重欠損マウスの作成を試みた。二重欠損マウスは個体レベルでは致死的であると考えられたが、8.5日胚より二重欠損線維芽細胞を単離することに成功した。この二重欠損細胞はXPC欠損細胞と同等の紫外線感受性、および不定期DNA合成活性を示したが、紫外線照射後のRNA合成の回復能は正常であったことから、XPC変異細胞と同様に転写と共役したヌクレオチド除去修復機構は正常で、ゲノム全体で働く副経路に特異的な欠損を持つことがわかった。さらに、この二重欠損細胞ではXPC蛋白質の発現量が著しく低下していたことから、RAD23ホモローグがXPC蛋白質の安定な発現に重要な役割を果たしていることが示された。以上の結果から、RAD23ホモローグはゲノム全体で機能するヌクレオチド除去修復機構に必須であると同時に、おそらく蛋白質分解系の制御を介して個体の発生、分化、成長においても重要な機能を果たしていることが強く示唆された。

  • C群色素性乾皮症(XPC)蛋白質の構造と機能
    菅澤 薫
    日本学術振興会, 科学研究費助成事業, 奨励研究(A), 理化学研究所, 1998 - 1999
    前年度までの組換え蛋白質を用いた無細胞系での実験から、C末端の125個のアミノ酸を欠失した変異XPC蛋白質は基本転写因子TFIIHとの相互作用に欠損が見られ、また無細胞ヌクレオチド除去修復反応においても不活性であることが明らかになった。そこで、この変異XPC蛋白質の細胞内での機能を解析する目的で、XP-C群細胞に変異遺伝子を導入して形質転換細胞株を樹立した。間接蛍光抗体染色により、上記のC末端欠失体、およびN末端の117個のアミノ酸を欠いた変異XPCはいずれも正常に核に移行できることを確認した。しかしながら、N末端欠失XPCを発現する細胞で紫外線抵抗性の回復が見られたのと対照的に、C末端欠失XPCを発現する細胞は親株のXPC欠損細胞と同等の紫外線感受性を示した。すなわち、無細胞系の結果と一致して、C末端部分はXPC蛋白質のヌクレオチド除去修復活性の発揮に必須であることが明らかになった。現在、C末端部分についてさらに細かい欠失変異体を作成しており、今後その構造機能相関を解析していく予定である。また、種々の変異XPC蛋白質を一過性に過剰発現して間接蛍光抗体染色を行なうことにより、XPC蛋白質の核移行に関わる配列をN末端付近に2ケ所同定した。 XPC蛋白質の活性が翻訳後修飾によって制御されている可能性を調べるため、まずXP-C群細胞にHA、またはFLAGタグを付加したXPC蛋白質のcDNAを導入して形質転換細胞株を単離した。これらの細胞株が正常細胞と同レベルのXPC蛋白質を発現していること、また紫外線抵抗性の回復からタグをつけたXPCが正常な機能を発揮できることを確認した。さらに、FLAGタグが特異的な免疫沈降に非常に有効であることを確かめたので、今後紫外線照射前後でのリン酸化の変動等を解析していく予定である。

  • ヌクレオチド除去修復機構におけるユビキチン蛋白分解系の役割
    菅澤 薫
    日本学術振興会, 科学研究費助成事業, 特定領域研究(A), 理化学研究所, 1998 - 1998
    出芽酵母RAD23のヒト・ホモローグであるhHR23B蛋白質は、ヌクレオチド除去修復(NER)においてDNA損傷の認識に関わるXPC蛋白質と強固な複合体を形成する。我々は、酵母two-hybrid screeningにより、26Sプロテアソーム・サブユニットの一つ、S5aが.hHR23B、およびもう一つRAD23ホモローグであるhHR23Aと相互作用することを見出している。組換え蛋白質の欠失変異体を用いたbinding assayにより、hHR23BではN末端のユビキチン相同配列、S5aの側ではマルチュビキチン鎖結合部位として同定されたC末端に近い領域が、この相互作用に必要であることがわかった。さらに、細胞抽出液を用いたグリセロール密度勾配遠心、およびプロテアソーム・サブユニットに対する抗体を用いた免疫共沈降実験から、細胞内においてもhHR23Bの少なくとも一部はプロテアソームに結合していることが示唆された。一方、二つのRAD23ホモローグのそれぞれについて、ノックアウトマウスを作成レた。mHR23A欠損マウスは外見上まったく正常であったが、mHR23B欠損マウスはメンデル則からの期待値の1/10程度の頻度でしか得られず、また個体サイズも野生型と比較して明らかに小さい。しかしながら、このマウスから単離したmHR23B欠損細胞のNER能は野生型と同様であった。このことは、NERに関しては二つのRAD23ホモローグ間に機能的互換性があること、また823Bは個体の発生、成長過程において、NER獣外の何らかの重要な機能を果たしていることを示している。

  • DNA複製、修復系を標的とした治療法の開発
    花岡 文雄, 菅澤 薫, 須藤 龍彦, 益谷 央豪
    日本学術振興会, 科学研究費助成事業, 重点領域研究, 1995 - 1995
    研究代表者と研究分担者は、DNA複製系及び修復系をターゲットとした新規抗がん剤の開発を目指して、以下に述べる研究を行なった。(1)前年度に引き続いて、既に確立されているSV40DNAの無細胞複製系、及び紫外線照射したSV40ミニ染色体を鋳型とする無細胞DNA修復系を用いて、100種ほどの放線菌培養上清から新たなDNA複製、及び修復阻害剤のスクリーニングを行なった。その結果、有意な阻害効果を示すサンプルを複数個、得ることが出来た。その中でDNA修復に阻害を示す4サンプルについて、DNAの損傷部位の上流および下流側に一本鎖切断を入れる反応を調べたところ、いずれもこの切断反応を阻害し、これらのサンプルがヌクレオチド除去修復反応の初期段階を阻害する活性を有していることが判明した。このステップの阻害剤は、これまで全く報告がなく、新規阻害剤の分離が期待される。(2)前年度までにDNA複製を強く阻害するものとして精製を行なっていたRK606については、構造決定の結果、大豆サポニンの一種、soyasaponin IIであることが判明した。類縁化合物のDNA複製阻害活性を比較したところ、アグリコン部分の他に、糖鎖の部分の構造も重要であること、また糖が3つ、分岐しない形で存在していると阻害活性が高いことが示された。DNA複製を阻害する化合物と、ワクシニアウイルスのdual-specific phosphatase,VH1フォスファターゼのヒトホモローグであるVHRフォスファターゼの阻害を示す化合物とが類似のスペクトルを示すことから、RK606の標的分子がフォスファターゼである可能性が示唆された。

  • 無細胞系を用いたp53による染色体複製制御機構の研究
    菅澤 薫
    日本学術振興会, 科学研究費助成事業, 奨励研究(A), 理化学研究所, 1994 - 1994
    バキュロウイルス・ベクター系を利用して昆虫細胞中で大量発現させたヒト野生型p53蛋白質をモノクローナルカラム抗体を用いて精製し、HeLa細胞の粗抽出液を用いたSV40DNAの無細胞複製系に添加して複製阻害を起こすことを確認した。この際、複製産物の解析から、p53蛋白質による複製阻害の作用点が主に複製開始段階にあることが示唆された。同様に4種類の変異型p53蛋白質(156Pro、248Trp、273His、285Lys)を昆虫細胞内で発現、精製したが、いずれも複製阻害活性を示さなかった。以上の結果は、精製蛋白質を用いた再構成複製系においても基本的に変わらなかった。モノクローナル抗体を用いた共沈降実験により、野生型p53蛋白質はSV40T抗原と試験管内で複合体を形成することが確かめられたが、4種類の変異型p53蛋白質は無細胞複製系の条件下では、いずれもSV40T抗原に結合しなかった。さらに、野生型p53蛋白質はSV40抗原の複製開始点への結合を阻害し、その結果としてT抗原による複製開始点を含む二重鎖DNA断片の一本鎖への巻き戻しを阻害するが、T抗原によって一本鎖環状M13DNA上の短いオリゴヌクレオチドが遊離される反応に対しては非常に弱い阻害効果しか示さないことがわかった。また、野生型p53蛋白質がSV40の複製開始点近傍に塩基配列特異的に結合することが報告されているが、この部分のDNA配列を欠失してもp53蛋白質による複製阻害が見られたことから、p53蛋白質の複製開始点近傍への結合は複製阻害にあまり重要でないと考えられた。以上の結果から、p53蛋白質によるSV40DNA複製阻害の機構は、主にSV40抗原との複合体形成によりT抗原の複製開始点への結合を阻害することにあると考えられる。

  • 細胞同期における染色体複製の制御機構に関する研究
    菅澤 薫
    日本学術振興会, 科学研究費助成事業, 奨励研究(A), 理化学研究所, 1993 - 1993
    SV40DNAの無細胞複製系に対する種々のプロテインキナーゼの影響を調べる目的で、まず精製された複製蛋白質に対して試験管内でリン酸化反応を行なってみた。その結果、MAPキナーゼやカゼインキナーゼIIがいくつかの複製蛋白質をリン酸化することが明らかとなった。しかしながら、これらのリン酸化反応によって各複製蛋白質の活性、および全体の複製反応に影響が見られるという結果は得られなかった。一方、ガン抑制遺伝子産物がG1期からS期への移行、染色体複製の開始を制御するという観点から、ヒトp53蛋白質の昆虫細胞における大量発現、ならびにモノクローナル抗体を用いた精製系を確立した。この系を用いて野生型ヒトp53蛋白質、およびヒトがん細胞から単離された数種の変異型p53蛋白質を精製し、SV40DNAの無細胞複製系に対する影響を解析した。その結果、野生型p53蛋白質SV40DNA複製を強く阻害したのに対して、変異型p53蛋白質はいずれも阻害を示さなかった。このSV40DNA複製の阻害活性と、それぞれのp53蛋白質のSV40T抗原との結合能の間には良い相関が見られ、実際に複製産物の解析から野生型p53による複製の阻害が開始段階の阻害であることが示唆された。現在、この組換えp53蛋白質を試験管内でリン酸化、および脱リン酸化した時に複製阻害活性に影響があるかどうか検討中である。

  • 哺乳類細胞のDNA修復機構と細胞周期制御の連関
    菅澤 薫
    日本学術振興会, 科学研究費助成事業, 重点領域研究, 理化学研究所, 1993 - 1993
    細胞周期におけるヌクレオチド除去修復活性の変動を解析する目的で、マウスFM3A細胞をnocodazoleでM期に同調後、解除して適当な時間培養したものをエルトリエーターで分画し、G1期の細胞を集めた。また、同様にFM3A細胞をaphidicolinでG1/S期境界に同調、及び解除することにより、エルトリエーター分画でS期とG2/M期の細胞を得た。これらの細胞より粗抽出液を調整し、無細胞修復系における活性を比較したところ、G2/M期の細胞抽出液がG1、及びS期の抽出液よりも2倍程度高い修復活性を示すことがわかった。さらに、マウスのcdc2キナーゼに変異を有するFM3A細胞の温度感受性突然変異株、tsFT210細胞を非許容温度でG2期に停止させたもの、及びこれをnocodazole存在下に許容温度に戻してM期に進めたものについて同様に修復活性を調べた。その結果、M期の細胞抽出液の方がG2期に停止した細胞抽出液よりも若干修復活性が高いという結果が得られた。現在、除去修復反応におけるcdc2キナーゼの関与、及び無細胞修復反応に伴う抽出液中のcdc2キナーゼの活性変動について検討中である。一方、哺乳類細胞のヌクレオチド除去修復自体に関与する因子を明らかにする目的で、C群色素性乾皮症の修復欠損を無細胞系で相補する蛋白質因子を同定し、その解析を進めているが、本年度においてはこの因子を構成する二種類のポリペプチドについてcDNAクローニングを行なった。

  • Study on Structure and Function of Mammalian DNA Replication Entyme
    HANAOKA Fumio, MASUTANI Chikahide, SUGASAWA Kaoru
    Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for General Scientific Research (B), The Institute of Phisical and Chemical Research (RIKEN), 1992 - 1993
    We isolated cDNA of the catalytic subunit of DNA polymerase alpha from tsFT20 cells, a temperature-sensitive mutant cell line derived from mouse FM3A cells. DNA sequence analysis revealed that the cDNA has a single mutation, a cytosine to thymine substitution that changes amino acid 1180 from serine to phenylalanine. We have also shown that tsFT20 cells could be rescued by transfection with the wild-type cDNA.In addition, we detected mutation sites in one spontaneous and six N-methyl-N'-nitro-N-nitrosoguanidine-induced growth revertants of tsFT20 cells. All revertant cell lines had a second point mutation adjacent to the first mutation site in tsFT20 cells. During activation of quiescent Swiss mouse 3T3 cells to proliferate, the levels of mRNA of the four subunits of the DNA polymerase alpha-primase complex increased before DNA synthesis. In order to analyze how the expression of these genes are controlled, we have isolated upstream region of these genes and determined their nucleotide sequence. There are 1-2 E2F-binding sequence and 10-14 dp palindromic sequence, and one AP1-binding motif in each upstream region. We overexpressed cDNAs of the DNA polymerase alpha-primase complex in E.coli or insect cells, purified the gene products and raised the specific antibodies against them. Co-precipitation experiments showed that 54K subunit has affinity to all other three subunits. We have also shown that 180K subunit has DNA polymerase activity and 46K subunit has primase activity.

  • Involvement of Chromosome in Regulation of DNA Replication and Repair
    HANAOKA Fumio, SUGASAWA Kaoru, MIYAZAWA Hiroshi
    Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for General Scientific Research (B), RIKEN (The Institute of Physical and Chemical Research), 1990 - 1991
    We have developed a call-free system for replication of SV40 minichromosomes with purified proteins. Since this reconstituted system lacked activity of de novo nucleosome assembly, we could specifically examine the behavior of parental histones during chromosome replication. Solution hybridization analyses suggested that the histones were not completely detached from but somehow associated with template DNA. Using strand-specific probes and MNase digested nascent mononucleosomal DNA, we obtained the results indicating that the parental histone octamers were segregated distributively between leading and lagging strands during the chromosome replication with purified proteifis. When SV40 chromosomes were replicated with topoI alone as a swivelase, the reaction produced shorter leading strands but those of mature size were accumulated in the reaction supplemented with topo II. These results indicate that topo II has a crucial role as a swivelase in the late stage of SV40 chromosome replication in vitro. On the other hand, we have developed a cell-free system supporting repair reactions on DNA organized into hucleosomes, that is, SV40 chromosomes. Standard reaction mixtures contained UV-irradiated SV40 chromosomes, unirradiated plasmid DNA, whole cell extracts of HeLa cells(Manley's extracts), ATP-regenerating system and several low molecular weight materials including[alpha-^<32>P]dCTP. After incubated at 30ﾟC, DNAs were isolated, digested with EcoRI and separated by agarose gel electrophoresis. Repair synthesis as well as nick-translation of DNAs were detected by autoradiography. DNA synthesis on SV40 DNA was dependent on doses of irradiated DNA. When we used cell extracts made from XP-A or XP-C cells in place of HeLa cell extracts, the UV-dependent DNA synthesis decreased remarkably. Mixing of XP-A and XP- C cell extracts restored the DNA synthesis to similar level as HeLa cell extracts. Thus our in vitro system appears to be useful for reconstituting at least some features of chromosomal DNA excision repair.

■ Industrial Property Rights
  • XPA pre-mRNAのプロセシングにおけるエクソン3のスキッピングを誘導するアンチセンスオリゴヌクレオチド
    菅澤 薫, 錦織千佳子, 高岡 裕, 酒井 恒, 辻本昌理子, 菅野亜紀
    特許特許第7033300号, 02 Mar. 2022
    Patent right

TOP